MXPA06007524A - Chewing gum comprising biodegradable polymers and having accelerated degradability - Google Patents

Abstract

The invention relates to chewing gum comprising at least one polymer, chewing gum ingredientsand enzymes, wherein at least on of said polymers forms a substrate for at least one of said enzymes. According to the invention the degradation of chewing gum comprising a combination of biodegradable polymers and enzymes is accelerated compared to chewing gum without enzymes. By incorporation of enzymes it is possible to obtain a chewing gum, which is relatively fast degrading compared to chewing gum , which is exposed to normal environmental conditions only.

Description

GUM OF BODY THAT COMPRISES BIODEGRADABLE POLYMERS AND THAT HAS ACCELERATED DEGRADABILITY FIELD OF THE INVENTION The present invention relates to chewing gum comprising biodegradable polymers and having an accelerated degradability.

BACKGROUND OF THE INVENTION It is generally recognized that chewing gum which is dropped in indoor or outdoor environments, gives rise to considerable discomfort and inconvenience due to the fact that the cast chewing gum adheres firmly to, for example, the surfaces of the street and the pavement and the shoes and clothes of the people who are present or who move in the environments. Adding substantially to such discomforts and drawbacks, is the fact that the chewing gum products currently available are based on the use of elastomeric and resinous polymers of natural or synthetic origin, which are substantially non-degradable in the medium. The authorities of the cities and others who are responsible for the cleanliness of the indoor and outdoor environments, therefore, have to exert considerable efforts to eliminate the chewing gum thrown, such efforts, however, are both costly and without results. satisfactory. Attempts have been made to reduce the discomfort associated with the widespread use of chewing gum, for example, by improving cleaning methods to make them more effective with respect to the removal of chewing gum remnants, or by incorporating antiadhesive agents in the formulations of chewing gum. However, none of these precautions has contributed significantly to solving the problem of pollution. The past two decades have seen an increased amount of interest lent to synthetic polyesters for a variety of applications, ranging from medical devices to rubber based. Many of these polymers are easily hydrolyzed to their monomeric hydroxy acids, which are easily eliminated by metabolic trajectories. Biodegradable polymers, for example, are anticipated as alternatives for traditional non-degradable or non-degradable plastics, such as poly (styrene), poly (isobutylene) and poly (methyl methacrylate). Thus, it has recently been described, for example, in US Pat. No. 5,672,367, that chewing gum can be made from certain synthetic polymers that have chemically unstable bonds in their polymer chains that can break under the influence of light or hydrolytically in components soluble in water and non-toxic. The claimed chewing gum comprises at least one degradable polyester polymer, obtained by the polymerization of cyclic esters, for example, based on lactides, glycolides, trimethylene carbonate and e-caprolactone. It is mentioned in this patent application that chewing gum made from such polymers that can be referred to as biodegradable are degradable in the environment. A problem related to the prior art, however, is that even biodegradable chewing gum may, under certain circumstances, have unsatisfactory degradability rates. It is an object of the invention to obtain a chewing gum with an even more rapid degradability than that described in the prior art.

SUMMARY OF THE INVENTION The invention relates to a chewing gum comprising at least one polymer, ingredients for chewing gum and enzymes, wherein at least one of the polymers forms a substrate for at least one of the enzymes.

According to the invention, the chewing gum polymers that form the substrates of the enzyme may be susceptible to enzymatic action in the sense that they may contain chemical bonds, the cleavage of which may be catalyzed by the enzymes. Therefore, according to the invention, the degradation of the chewing gum comprising a combination of polymers and enzymes can be accelerated in comparison with the degradation of the chewing gum without the enzymes. By incorporating enzymes, it is possible to obtain a chewing gum, which degrades relatively quickly compared to chewing gum, which is exposed to normal environmental conditions only. The degradation according to the invention can lead to the disintegration of the chewing gum into smaller pieces, oligomers, trimers, dimers and finally monomers and smaller products. If the extent of the degradation is partial or total, it depends on the time elapsed, the pH, the humidity, the temperature and, in addition, the chemical, physical and environmental factors. In one embodiment of the invention, the chewing gum includes a center filling. In the manufacture of a chewing gum according to the invention, the enzymes can be incorporated in the filling of the center and subsequently mixed in all parts of the chewing gum during the chewing process, whereby the enzymatic catalytic effect can be obtained in degradation. The incorporated enzymes can be added as, for example, liquid or powder or contained in encapsulation. In another embodiment of the invention, the chewing gum includes a coating. Thus, the enzymes can be incorporated into the chewing gum coating and still result in the desired effect after the chewing of the chewing gum, which to a certain degree, will result in a mixing of at least some of the available enzyme concentration of the coating with the substrate, that is, the chewing gum polymer. In this context, a coating of the chewing gum or for example, a filling of the center or a part of a filling of the center is considered as part of the chewing gum, although most applications refer to a chewing gum and the coating as two separate parts of the tablet. In one embodiment of the invention, the chewing gum ingredients comprise sweeteners and flavors. In one embodiment of the invention, the ingredients of the chewing gum comprise additional softeners and additives.

In one embodiment of the invention, the polymer forms a base for chewing gum. In one embodiment of the invention, the polymer comprises at least one copolymer. In one embodiment of the invention, the polymer is polymerized from at least two different monomers, each comprising 1-99%. The copolymerization provides a polymer having a relatively low crystallinity, whereby the amorphous regions provide improved degradability. In one embodiment of the invention, the polymer comprises at least one biodegradable polymer. In one embodiment of the invention, the chewing gum comprises at least one biodegradable polymer and at least one type of enzyme. According to the invention, a chewing gum comprising a biodegradable polymer and enzymes exhibits improved degradability. The application of at least one polymer generally considered to be biodegradable can increase the effect of the incorporated enzymes in the sense that the biodegradable polymers can have a high degree of susceptibility to enzymatic influence. Some useful biodegradable polymers can be copolymerized from different monomers, copolymerization which can facilitate amorphous regions and consequently, biodegradable polymers can be even more susceptible to enzymatic attack. In one embodiment of the invention, the biodegradable polymer comprises at least one biodegradable elastomer. In one embodiment of the invention, the biodegradable polymer comprises at least one plasticizer of the biodegradable elastomer. In one embodiment of the invention, at least one of the biodegradable polymer comprises at least one polyester polymer obtained by the polymerization of at least one cyclic ester. Preferably, such a polymerization is ring opening polymerization of cyclic esters, which provide an aliphatic polyester polymer, which is more susceptible to enzymatic degradation than aromatic polyesters. By polymerizing the rings, such as lactide, the final degradation product is known as lactic acid, which is not harmful to the environment and in the case of slight degradation in the chewing gum before it is discarded, The lactic acid can even have a positive effect on the flavor in the fruit flavored chewing gum. In one embodiment of the invention, at least one of the biodegradable polymer comprises at least one polyester polymer obtained by the polymerization of at least one alcohol or derivative thereof and at least one acid or a derivative thereof. In one embodiment of the invention, at least one of the biodegradable polymer comprises at least one polyester obtained by the polymerization of at least one compound selected from the group of cyclic esters, alcohols or derivatives thereof and carboxylic acids or derivatives thereof. In one embodiment of the invention, the polyester obtained by the polymerization of at least one cyclic ester is at least partially derived from the α-hydroxy acids, such as lactic and glycolic acids. In one embodiment of the invention, the polyester obtained by the polymerization of at least one cyclic ester is at least partially derived from α-hydroxy acids and wherein the obtained polyesters comprise at least 20 mol% of a-hydroxy acid units, so preferred, at least 50% by mole of a-hydroxy acid units and more preferably, at least 80% by mole of a-hydroxy acid units. In one embodiment of the invention, the one or more cyclic esters are selected from the groups of glycolides, lactides, lactones, cyclic carbonates or mixtures thereof. In one embodiment of the invention, the lactone monomers are selected from the group of e-caprolactone, d-valerolactone, β-butyrolactone and β-propiolactone. It also includes e-caprolactones, d-valerolactones,? -butyrolactones or β-propiolactones that have been substituted with one or more alkyl or aryl substituents on any non-carbonyl carbon atoms along the ring, including compounds in which two or more substituents are contained in the same carbon atom. In one embodiment of the invention, the carbonate monomer is selected from the group of trimethylene carbonate, 5-alkyl-1,3-dioxan-2-one, 5,5-dialkyl-1,3-dioxan-2-one or 5-alkyl-5-alkylcarbonyl-l, 3-dioxan-2-one, ethylene carbonate, 3-ethyl-3-hydroxymethyl, propylene carbonate, trimethylpropane monocarbonate, carbonate of 4,6-dimethyl-l, 3- propylene, 2,2-dimethyltrimethylene carbonate and 1,3-dioxepan-2-one and mixtures thereof. In one embodiment of the invention, cyclic ester polymers and their copolymers resulting from the polymerization of cyclic ester monomers include, but are not limited to: poly (L-lactide); poly (D-lactide); poly (D, L-lactide); poly (mesolactide); poly (glycolide); poly (trimethylene carbonate); 52-372 poly (epsilon-caprolactone); poly (L-lactide-co-D, L-lactide); poly (L-lactide-co-meso-lactide); poly (L-lactide-co-glycolide); poly (L-lactide-co-trimethylene carbonate); poly (L-lactide-co-epsilon-caprolactone); poly (D, L-lactide-co-meso-lactide); poly (D, L-lactide-co-glycolide); poly (D, L-lactide-co-trimethylene carbonate); poly (D, L-lactide-co-epsilon-caprolactone); poly (meso-lactide-co-glycolide); poly (trimethylene meso-lactide-co-carbonate); poly (meso-lactide-co-epsilon-caprolactone); poly (trimethylene glycolide-co-carbonate); poly (glycolide-co-epsilon-caprolactone). In one embodiment of the invention, the polymer has a degree of crystallinity in the range of 0 to 95% and more preferably, 0 to 70%. Preferably, the chewing gum according to the invention comprises polymers having regions of low crystallinity, due to the fact that the degradation catalyzed by the enzyme can occur more easily in regions of polymers having low crystallinity, than in regions that It has greater crystallinity. In some cases, the enzymatic degradation can degrade the amorphous regions and leave the partially degraded polymer having only crystalline regions. In one embodiment of the invention, at least one of the polymer has amorphous regions. 52-372 In one embodiment of the invention, the polymer is aliphatic. In one embodiment of the invention, the molecular weight of the polymer is in the range of 500-500000 g / mol, preferably within the range of 1500-200000 g / mol of Mn. In one embodiment of the invention, at least one of the enzymes catalyses the degradation of at least one polymer. In one embodiment of the invention, the chewing gum, after use, is partially disintegrated due to the influence of the enzymes. The piece of chewing gum that remains after use changes its structure, due to the enzymatic influence, and experiments have shown that the piece of chewing gum, when certain conditions are met, is released from the surfaces to which it joins The piece. In other words, non-adhesiveness can be obtained even without any visual disintegration of the piece. In one embodiment of the invention, at least one of the enzymes influences the polymer substrate with a partial disintegration of the chewing gum as a result. In one embodiment of the invention, at least one of the enzymes influences the polymer substrate with a partial disintegration and a collapsing structure. 52-372 chewing gum, as a result. The piece of chewing gum that remains after use may, due to enzymatic catalysis, be partially degraded, so that the remaining parts are moronas that can be easily removed externally by environmental factors, such as climatic conditions such as rain and in the interior, by physical factors such as a brush or a vacuum cleaner. In one embodiment of the invention, at least one of the enzymes is catalyzing, after use of the chewing gum, the degradation of the polymer substrate, until the polymer is completely degraded. When complete degradation is obtained, the polymer residues are basic compounds, which can enter the cycle in nature. In one embodiment of the invention, at least one of the enzymes is active in atmospheric air and pressure and is accelerating the degradation of the polymer. The natural external environment is an important factor for enzymatic degradation to occur. Enzymatic activity must be optimal under atmospheric conditions. In one embodiment of the invention, at least one of the enzymes is contained in the chewing gum, the gum base, the center filler or the coating. 52-372 According to the invention, the enzymes can be placed in the chewing gum parts and still provide an acceleration of the degradation subsequent to the mixing of the enzymes and the polymer substrate during chewing. In an embodiment of the invention, at least one of the enzymes is accelerating the degradation of the polyester obtained by the ring opening polymerization of at least one cyclic ester. In one embodiment of the invention, at least one of the enzymes is accelerating the degradation of the polyester obtained by the polymerization of at least one alcohol or a derivative thereof and at least one acid or a derivative thereof. Studies have shown that the polyesters belonging to these two polyester groups were especially susceptible to the catalytic influence of the enzymes in their degradation. Therefore, the application of these polymers in the chewing gum containing the enzyme can provide a particularly degradable chewing gum. In one embodiment of the invention, the chewing gum comprises at least one polyester obtained by ring-opening polymerization of at least one cyclic ester and at least one polyester obtained by the 52-372 polymerization of at least one alcohol or a derivative thereof, and at least one acid or a derivative thereof. In one embodiment of the invention, the chewing gum of the invention has a water content of less than 10%, preferably less than 5%, preferably less than 1% by weight and even more preferably, lower than 0.1% by weight. Provided that the chewing gum has not been used, it is important to keep the water content low, to prevent the chewing gum from degrading, for example, a hydrolytic degradation catalyzed by the hydrolase enzymes. In one embodiment of the invention, the chewing gum is capable of absorbing water in an amount of at least 0.1% by weight, preferably at least 5% by weight; more preferably at least 10% by weight, even more preferably, at least 20% by weight and even more preferably at least 40% by weight. When the water is absorbed in the chewing gum, the conditions for hydrolytic degradation to take place are improved. The absorption of water is an important parameter to control the degradability of biodegradable chewing gum. This is especially important when the enzymes applied are hydrolases. In one embodiment of the invention, the rubber of 52-372 chewing comprises a filling in an amount of 0 to 80%. The content of the filler can provide the chewing gum with a higher capacity for water uptake, and therefore, more favorable conditions for enzymatically accelerated degradation, such as, for example, hydrolysis and oxidation. In one embodiment of the invention, the concentration of the enzymes is in the range of 0. 0001% by weight to 50% by weight of the chewing gum. A high concentration of the enzyme results in further degradation with respect to speed and completeness.

In addition, a high concentration will be more likely to result in an increased concentration of the enzymes in the chewed gum. However, if the concentration of the enzyme is very high, enzymatic degradation can be prevented. In one embodiment of the invention, the concentration of the enzymes is in the range of 0.001% by weight to 10% by weight of the chewing gum. In one embodiment of the invention, the concentration of the enzymes is in the range of 0.01% by weight to 5% by weight of the chewing gum. In one embodiment of the invention, the amount of the enzymes is in the range of 0.0001 to 80% by weight relative to the amount of base for gum in the gum. 52-372 chew. In one embodiment of the invention, the amount of the enzymes is in the range of 0.001 to 40% by weight relative to the amount of the gum base in the chewing gum. In one embodiment of the invention, the amount of the enzymes is in the range of 0.1 to 20% by weight relative to the amount of the gum base in the chewing gum. In one embodiment of the invention, at least one of the enzymes is selected from the group consisting of oxidoreductases, transferases, hydrolases, lyases, isomerases and ligases. In one embodiment of the invention, at least one of the enzymes is an oxidoreductase. In one embodiment of the invention, at least one of the enzymes is a hydrolase. In one embodiment of the invention, at least one of the enzymes is a lyase. In one embodiment of the invention, at least one of the hydrolase enzymes is acting on the ester linkages. In one embodiment of the invention, at least one of the hydrolase enzymes is a glycosylase. In one embodiment of the invention, at least one of the hydrolase enzymes is acting on the ether linkages. 52-372 In one embodiment of the invention, at least one of the hydrolase enzymes is acting on carbon-nitrogen bonds. In one embodiment of the invention, at least one of the hydrolase enzymes is acting on the peptide bonds. In one embodiment of the invention, at least one of the hydrolase enzymes is acting on the acid anhydrides. In an embodiment of the invention, at least one of the hydrolase enzymes is acting on carbon-carbon bonds. In one embodiment of the invention, at least one of the hydrolase enzymes is acting on the halide bonds, the phosphorus-nitrogen bonds, the sulfur-nitrogen bonds, the carbon-phosphorus bonds, the sulfur-sulfur bonds or the carbon-sulfur bonds. In one embodiment of the invention, at least one of the enzymes is selected from the group of lipases, esterases, depolymerases, peptidases and proteases. Due to the polymeric nature of the substrate according to the invention, such enzymes, as different depolymerases are suitable for degradation, due to their ability to catalyze the degradation of different types of polymer. Lipases can also be used to 52-372 the degradation of the polymer, since they are able to cleave the bonds found in the oil and solid phases. With respect to some other preferred polymers containing ester linkages, the most convenient enzymes may fall generally in the esterase group. Similarly, it has been found that peptidases and proteases cleave various polymeric substrates. In one embodiment of the invention, at least one of the enzymes is an endoenzyme. In one embodiment of the invention, at least one of the enzymes is an exoenzyme. In one embodiment of the invention, at least one of the enzymes has a molecular weight of 2 to 1000 kDa, preferably 10 to 500 kDa. In one embodiment of the invention, at least two of the enzymes are combined. In the present context, a combination of at least two enzymes means that these enzymes are added in the same chewing gum. By the addition of at least two different types of enzymes, for example, two different hydrolases or for example, a hydrolase and an oxidoreductase, in the same chewing gum, the enzymatic influence on the degradation can be significantly improved. In one embodiment of the invention, at least one of 52-372 enzymes requires a cofactor to carry out its catalytic function. In one embodiment of the invention, at least one of the enzymes is incorporated into the chewing gum. In one embodiment of the invention, at least one of the enzymes is incorporated into the gum base. In one embodiment of the invention, at least one of the enzymes is incorporated into the coating. In nature, through environmental factors, degradation progresses mainly on the surface of, for example, polymers, but by incorporating the enzymes in the chewing gum, the degradation proceeds from the inside as well, so the disintegration of the Gum may start at an earlier stage during degradation. In one embodiment of the invention, at least one of the enzymes has an optimum activity in the pH range of 1.0 to 11.0, preferably 4.0 to 8.0 and more preferably 4.0 to 6.0. In one embodiment of the invention, at least one of the enzymes has an optimal activity at temperatures ranging from -10 to 60 ° C, preferably from 0 to 50 ° C, more preferably from 5 to 40 ° C. ° C and even more preferably from 10 to 35 ° C. In one embodiment of the invention, at least one of 52-372 enzymes have an optimum activity at a relative humidity in the range of 10 to 100% RH, preferably 30 to 100% RH. Preferably, the enzymatic influence of the enzymes on chewing gum polymer degradation is considerable under the chemical and physical conditions, typically found in the natural environment, where the chewing gum may be deposited. In one embodiment of the invention, the chewing gum is prepared by a one-step process. In one embodiment of the invention, the chewing gum is prepared by a two-step process. In one embodiment of the invention, the chewing gum is prepared by a continuous mixing process. In one embodiment of the invention, the chewing gum is compressed and prepared by the use of compression techniques. In addition, the invention relates to the use of at least one enzyme for the degradation of biodegradable chewing gum. In one embodiment of the invention, at least one enzyme comprises hydrolases. In addition, the invention relates to at least one biodegradable polymer that is at least partially degraded by means of at least one enzyme. 52-372 In one embodiment of the invention, the enzyme is mixed together with at least one biodegradable polymer by chewing.

FIGURES The invention will now be described with reference to the following figures, which illustrate the formation of degradation products, as measured by upper space GC / MS: Figure 1 illustrates the formation of a compound a and b in chewing gum which contains glucose oxidase. Figure 2 illustrates the formation of a compound a and b in the chewing gum containing neutrase. Figure 3 illustrates the formation of a compound a and b in chewing gum containing bromelain. Figure 4 illustrates the formation of a compound a and b in chewing gum containing trypsin.

DETAILED DESCRIPTION The present invention relates to a chewing gum comprising biodegradable polymers, chewing gum ingredients and enzymes. By these means, a chewing gum can be provided, wherein the polymers constitute the substrates for the enzymes and consequently, they are at least partially degraded. 52-372 According to the invention, a method is obtained through which the biodegradable polymers in chewing gum can be degraded by means of enzymes, which can result in an increased degradation of the polymer, with respect to the speed and degree of degradation, compared to non-enzymatic degradation. It was discovered that the use of enzymes for the purpose of chewing gum polymer degradation, can advantageously facilitate the possibility of including polymers which under normal circumstances are considered as having a limited biodegradability and therefore, to some degree they are avoided in biodegradable chewing gum compositions. The favorable influence on the desired texture that these polymers may have may be due to the use of enzymes that is obtained without compromising the degradability of the chewing gum. In one embodiment of the invention, the degradation of a biodegradable polymer is provided and / or accelerated when applied under environmental conditions under which degradation would not occur if it is not triggered. If chewing gum is placed on the ground in outdoor environments, there are many chemical, physical and biological factors, so the degradation of biodegradable polymers is facilitated. But if it falls, for example, on pavements or in the interior, the chewing gum may not find the circumstances required for degradation. In that case, even biodegradable chewing gum can be a drawback. A solution according to the present invention facilitates the acceleration of degradation in environments where the conditions are only slightly degrading. The presence of enzymes makes the progress of the degradation process faster, than if the only influences were the physical and / or chemical factors in the surroundings. According to a preferred definition of biodegradability according to the invention, biodegradability is a property of certain organic molecules, whereby, when they are exposed to the natural environment or placed inside a living organism, they can react through a process enzymatic or microbial, often in combination with a chemical process such as hydrolysis, to form simpler compounds, and finally carbon dioxide, nitrogen oxides, methane, water and the like. In the present context, the term "biodegradable polymers" means environmentally or biologically degradable polymer compounds, and refers to the components of the base for gum, which, after 52-372 waste chewing gum, are able to undergo physical, chemical and / or biological degradation, so that the waste of the discarded chewing gum is more easily removed from the waste site or finally disintegrates into pieces or particles , which are no longer recognized as remnants of chewing gum. The degradation or disintegration of such degradable polymers can be effected or induced by physical factors such as temperature, light, humidity, etc., by chemical factors such as oxidative conditions, pH, hydrolysis, etc., or by biological factors such as microorganisms and / or enzymes. The degradation products can be larger oligomers, trimers, dimers and monomers. Preferably, the final products of the degradation are small inorganic compounds such as carbon dioxide, nitrogen oxides, methane, ammonia and water. In some embodiments, all of the polymer components of the gum base are environmentally or biologically degradable polymers. In the present context, the term "enzyme" is used in the same sense as it is used within the technique of biochemistry and molecular biology. Enzymes are biological catalysts, typically proteins, but non-proteins with enzymatic properties have been discovered. Enzymes originate from living organisms where they act as catalysts and therefore regulate the rate at which chemical reactions proceed without being altered themselves in the process. The biological processes that occur within all living organisms are chemical processes, and enzymes regulate most of them. Without the enzymes, many of these reactions would not take place at a noticeable speed. Enzymes catalyze all aspects of cellular metabolism. This includes the conservation and transformation of chemical energy, the construction of cellular macromolecules of smaller precursors and the digestion of food, in which large molecules of nutrients such as proteins, carbohydrates and fats are broken into smaller molecules. Enzymes generally have valuable industrial and medical applications. The fermentation of wine, the raising of bread, the coagulation of cheese, and the preparation of beer have been practiced since the beginning of time, but it was not until the 19th century when it was understood that these reactions are the result of activity catalytic of enzymes. Since then, enzymes have assumed an importance that increases in industrial processes that involve organic chemical reactions. Research and development of 52-372 enzymes are still in progress and new applications of the enzymes are discovered. Synthetic polymers are often considered difficult to degrade by enzymes and theories have been proposed to explain this phenomenon, suggesting that enzymes tend to attack the ends of chains and that the ends of the chains of man-made polymers tend to to be very deep in the polymer matrix. However, the experiments according to the present invention surprisingly showed that the effect of adding the enzymes in the chewing gum apparently was that the chewing gum polymers experienced more degradation. Like catalysts, enzymes can generally increase speed to achieve a balance between the reactants and the products of chemical reactions. According to the present invention, these reagents comprise polymers and different degrading molecules such as water, oxygen or other reactive substances, which can enter the vicinity of the polymers, while the products comprise oligomers, trimers, dimers, monomers and products of smaller degradation. When the reactions are catalyzed by the enzyme, at least one of the reagents forms a substrate for at least one enzyme, which means that a temporary binding arises between the reagents, ie, the substrates of the enzyme and 52-372 the enzyme. In different ways, this union makes the reaction proceed more quickly, for example, leading the reactants to conformations or positions that favor the reaction. An increase in the rate of the reaction due to the enzymatic influence, i.e., catalysis, generally occurs due to a decrease in the barrier of the activation energy for the reaction to take place. However, the enzymes do not change the difference in the free energy level between the initial and final states of the reactants and the products, since the presence of the catalyst does not have an effect on the equilibrium position. When a catalytic process has been completed, the enzyme releases the product or products and returns to its original state, ready for another substrate. The temporary binding of one or more molecules of the substrate occurs in regions of the enzymes called the active sites and may comprise, for example, hydrogen bonds, ionic interactions, hydrophobic interactions or weak covalent bonds. In the complex tertiary structure of the enzymes, an active site can take the form of a pocket or slit, which fits with substrates or particular parts of the substrates. Some enzymes have a very specific mode of action, while others have a broad specificity and can catalyze a series of substrates. Basically, the 52-372 molecular conformation is important for the specificity of the enzymes, and can become active or inactive by varying the pH, temperature, solvent, etc. Even some enzymes require coenzymes or other cofactors that are present in order to be effective, in some cases forming the association of complexes in which a coenzyme acts as a donor or acceptor of a specific group. Sometimes enzymes can be specified as endo-enzymes or exo-enzymes, thus referring to their mode of action. According to this terminology, exoenzymes can successively attack the ends of the chains of the polymer molecules, and therefore, for example, release terminal residues or single units, while endo-enzymes can attack half of the chain and act on the inner bonds within the polymer molecules, thereby cleaving the larger molecules into smaller molecules. Generally, enzymes can be obtained as liquids or powders and eventually, they can be encapsulated in various materials. At present, several thousand different enzymes have been discovered and are being discovered more continuously, thus, the number of known enzymes is increasing still. For this reason, the Nomenclature Committee of the International Union of Biochemistry and 52-372 Molecular Biology (NC-IUBMB). { Nomenclature Committee of the International Union of Biochemistry and Molecular Biology), has established a rational system of naming and numbering. In the present context, the names are used in accordance with the recommendations considered by the NC-IUBMB. The general principles in the manufacture of a method according to the invention will now be described together with a general description of the product obtained. Two quite different aspects of the invention will now be briefly summarized. A first aspect according to one embodiment of the invention is to treat the possibility of increasing the degradability of a biodegradable chewing gum, applied in a chewing gum having a polymeric matrix comprising only or in part, biodegradable polymers. A second quite different aspect is better to facilitate the use of conventional polymers or biodegradable polymers, which without any catalyzing enzyme are less suitable for the application with respect to, for example, the rate of degradation. Briefly, those and other additional aspects are obtained by applying enzymes in the chewing gum, than the triggers and catalysts of the degradation. In other words, according to the invention, at least one 52-372 biodegradable polymer of a chewing gum forms a paired substrate with a suitable enzyme. Several different criteria must be considered when determining which enzymes should be matched with which polymers, by which processes, etc. According to four preferred embodiments of the invention, a biodegradable chewing gum containing enzymes can be prepared by a conventional two-step batch process, a less-used but quite promising one-step process or, for example, continuous batching , for example, by means of an extruder and the fourth preferred embodiment is to prepare the chewing gum by using compression techniques. The two-step process comprises separately manufacturing a gum base and subsequently mixing the gum base with additional ingredients of the chewing gum. Several other methods can also be applied. Examples of two-step processes are well described in the prior art. An example of a one-step process is described in WO 02/076229 Al, included herein by reference. Examples of continuous mixing methods are described in US 6 017 565 A, US 5 976 581 and US 4 968 511, included herein by reference. Examples of processes for producing compressed chewing gum are described in US 4405647, US 4753805, WO 52-372 8603967, EP 513978, US 5866179, WO / 97/21424, EP 0 890 358, DE 19751330, US 6,322,828, PCT / DK03 / 00070, PCT / DK03 / 00465, included herein by reference. If a two-step process is applied, care must be taken, for example, to avoid too much heating of the applied enzymes. This can be done, for example, by mixing the enzymes applied in the chewing gum in the second step, that is, the step where the gum base is mixed with the chewing gum ingredients. If a one-step process is applied, the same problem must be observed, although the one-step process, in some way, seems to be quite adequate for the purpose and in some processes, the control of temperature and cooling can, in fact, , avoid yourself. If a complete mixing method is applied, again, active cooling and heating should be carefully controlled to avoid destruction or damage described above of the applied enzymes. Turning now to one of the several main embodiments of the invention, chewing gum will now be described in more general terms. First of all, the chewing gum comprises a polymeric composition, which is partially or solely based on biodegradable polymers. These polymers 52-372 are, as is the case with conventional non-degradable chewing gum, the components of chewing gum that provide the texture and "chewing" properties of a chewing gum. The lists of suitable and preferred polymers according to the invention are described below (at the end of the description). In addition, the chewing gum comprises additional additives applied to obtain the desired refinement of the chewing gum mentioned above. Such additives may, for example, comprise softeners, emulsifiers, etc. Lists of such suitable and preferred additives are described below (at the end of the description). In addition, the chewing gum further comprises ingredients applied to obtain the desired flavor and properties of the chewing gum mentioned above. Such ingredients may, for example, comprise sweeteners, flavors, acids, etc. Lists of such suitable and preferred ingredients are described below (at the end of the description). It should be emphasized that the additives and ingredients mentioned above can interact in function. As an example, the flavors can, for example, be applied as or act as softeners in the complete system. A strict distinction between 52-372 additives and ingredients can not be established in typical fashion. In addition, a coating can be applied for the complete or partial encapsulation of the center of the obtained chewing gum. In the present context, the coating and filling of the center are considered as a whole, thus, the use of the term "chewing gum" includes both the body of the chewing gum and an optional coating. Examples of different coatings are described below (at the end of the description). The advantages according to the invention are that partial disintegration or improvement in the non-adhesiveness of the chewing gum piece can be obtained. An additional explanation of the advantages is provided in two separate examples. An example is when the enzymatic influences result in a partial disintegration and a crumbling structure of the piece, thus releasing the ingredients that form the piece of the surface. Another example deals with a situation in which the piece of chewing gum changes its structure due to the enzymatic influence and where experiments have shown that the piece of chewing gum, when certain conditions are met, is released from the surfaces to which the piece is attached. In other words, this non-adhesive property can be obtained even without any 52-372 visual disintegration of the piece. It is a further advantage according to the invention, that complete dissolution can be obtained, which means that the polymer residues can enter the cycle in nature. The incorporation of enzymatic influences results in completely biodegradable chewing gum polymers. In accordance with the general principles in the manufacture of a modality according to the invention, suitable examples of polymers, enzymes and ingredients of chewing gum will be explained below. Suitable examples of environmentally or biologically degradable polymers for the base for chewing gum, which may be applied in accordance with the gum base of the present invention, include polyesters, poly (ester carbonates), polycarbonates, polyester amides, polypeptides , amino acid homopolymers such as polylysine, and proteins, including derivatives thereof, such as, for example, protein hydrolysates, including a hydrolyzate of zein. Particularly useful compounds of this type include polyester polymers obtained by the polymerization of one or more cyclic esters, such as lactide, glycolide, trimethylene carbonate, d-valerolactone, β-propiolactone and e-caprolactone, and polyesters obtained by the 52-372 polycondensation of a mixture of polyacids and open chain polyols, for example, adipic acid and di (ethylene glycol). Hydroxycarboxylic acids such as 6-hydroxycaproic acid can also be used to form the polyesters or can be used in conjunction with mixtures of polyacids and polyols. Such degradable polymers can be homopolymers, copolymers or terpolymers, including block and graft copolymers. Particularly useful biodegradable polyester compounds produced from the cyclic esters can be obtained by ring-opening polymerization of one or more cyclic esters, including glycolides, lactides, lactones and carbonates. The polymerization process can take place in the presence of at least one suitable catalyst such as metal catalysts, of which the stannous octoate is a non-limiting example and the polymerization process can be initiated by initiators such as polyols, polyamines or other molecules with multiple hydroxyl groups or other reactive groups and mixtures thereof. Accordingly, particularly useful biodegradable polyesters produced through the reaction of at least one alcohol or a derivative thereof and at least one acid or a derivative thereof, can be prepared 52-372, generally by a step polymerization of alcohol diols, tri or with greater functionality, or esters thereof with aliphatic or aromatic di, tri or higher functional carboxylic acids or esters thereof. Likewise, hydroxy acids or anhydrides or halides of polyfunctional carboxylic acids can also be used as monomers. Polymerization can involve polyesterification or direct transesterification and can be catalyzed. The use of branched monomers suppresses the crystallinity of polyester polymers. The mixing of different monomer units along the chain also suppresses the crystallinity. In order to control the reaction and the molecular weight of the resulting polymer, it is possible to stop the polymer chains by the addition of monofunctional alcohols or acids and / or to use a stoichiometric imbalance between the acid groups and the alcohol groups or the derivatives of any of them. Also, the addition of aliphatic carboxylic acids or long chain aromatic monocarboxylic acids can be used to control the degree of branching in the polymer, and conversely, multifunctional monomers are sometimes used to create branching. In addition, after the polymerization, monofunctional compounds can be used to cover the end of the free hydroxyl and carboxyl groups.

In addition, the polyfunctional carboxylic acids are solids with a high melting point, which have a very limited solubility in the reaction medium of the polycondensation. Frequently, esters or anhydrides of polyfunctional carboxylic acids are used to overcome this limitation. Polycondensations involving carboxylic acids or anhydrides produce water as the condensate, which requires that high temperatures be eliminated. Thus, polycondensations involving the transesterification of the ester of a polyfunctional acid are often the preferred process. For example, the dimethyl ester of terephthalic acid can be used in place of the terephthalic acid itself. In this case, methanol is condensed more than water, and the former can be removed more easily than water. Usually, the reaction is carried out in the volume (not the solvent) and high temperatures and vacuum are used to remove the by-product and bring the reactions to term. In addition to an ester or anhydride, a halide of a carboxylic acid may also be used, under certain circumstances. Additionally, for the preparation of type 1 polyesters, preferred polyfunctional carboxylic acids or derivatives thereof are saturated or unsaturated aliphatics or aromatics and contain from 2 to 100 carbon atoms and more 52-372 preferred, from 4 to 18 carbon atoms. In the polymerization of this type of polyester, some applicable examples of the carboxylic acids, which may be employed as such or as derivatives thereof, include aliphatic polyfunctional carboxylic acids, such as oxalic, malonic, citric, succinic, malic, tartaric, fumaric, maleic, glutaric, glutamic, adipic, glucaric, pimelic, suberic, azelaic, sebacic, dodecandioic, etc., and cyclic aliphatic carboxylic acids, such as cyclopropane dicarboxylic acid, cyclobutan dicarboxylic acid, cyclohexane dicarboxylic acid, etc., and acids aromatic polyfunctional carboxylic acids, such as terephthalic, isophthalic, phthalic, trimellitic, pyromellitic and naphthalene 1,4-, 2,3-, 2,6-dicarboxylic acids and the like. For the purpose of illustration and not limitation, some examples of carboxylic acid derivatives include hydroxy acids such as 3-hydroxy propionic acid and 6-hydroxycaproic acid and anhydrides, halides or acid esters, for example, dimethyl or diethyl esters, corresponding to the aforementioned acids, which means esters such as dimethyl or diethyl oxalate, malonate, succinate, fumarate, maleate, glutarate, adipate, pimelate, suberate, azelate, sebacate, dodecandioate, terephthalate, isophthalate, phthalate, etc. Generally speaking, methyl esters are sometimes more preferred than ethyl esters due to the fact that alcohols with a higher boiling point are more difficult to remove than alcohols with a low boiling point. In addition, the usually preferred polyfunctional alcohols contain from 2 to 100 carbon atoms, such as, for example, polyglycols and polyglycerols. In the polymerization process of polyester of type 1, some applicable examples of alcohols, which may be employed as such or as derivatives thereof, include polyols such as ethylene glycol, 1,2-propanediol, 1,3-propanediol, 1,3 -butanediol, 1,4-butanediol, 1,6-hexanediol, diethylene glycol, 1,4-cyclohexanediol, 1,4-cyclohexanedimethanol, neopentyl glycol, glycerol, trimethylolpropane, pentaerythritol, sorbitol, mannitol, etc. For purposes of illustration and not limitation, some examples of alcohol derivatives include triacetin, glycerol palmitate, glycerol sebacate, glycerol adipate, tripropionin, etc. In addition, with respect to the polymerization of polyesters of this type, the compounds that stop the chains used are sometimes monofunctional compounds. They are preferably monohydric alcohols containing 1-20 carbon atoms or monocarboxylic acids containing 2-26 carbon atoms. The 52-372 general examples are alcohols or medium or long chain fatty acids, and specific examples include monohydric alcohols such as methanol, ethanol, butanol, hexanol, octanol, etc., and lauryl alcohol, myristyl alcohol, cetyl alcohol, stearyl alcohol , stearic alcohol, etc., and monocarboxylic acids such as acetic, lauric, myristic, palmitic, stearic, arachidic, cerotic, dodecylenic, palmitoleic, oleic, linoleic, linolenic, erucic, benzoic, naphthoic and substituted naphthoic acids, acid l- methyl-2 naphthoic and 2-isopropyl-1-naphthoic acid, etc. In addition, an acid catalyst or a transesterification catalyst is typically used in the polymerization of polyesters of this type and non-limiting examples thereof are metal catalysts such as manganese, zinc, calcium, cobalt or magnesium acetates, and sodium oxide. antimony (III), germanium oxide or halide and tetraalkoxygermanium, titanium alkoxide, zinc or aluminum salts. Suitable enzymes according to the general principles in the manufacture of a modality within the scope of the present invention, can be identified as belonging to six classes according to their function: Oxidoreductases, transferases, hydrolases, lyases, isomerases and ligases. The oxidoreductases 52-372 catalyze the oxidation-reduction reactions, and the oxidized substrate is considered as hydrogen or an electron donor. Transferases catalyze the transfer of functional groups from one molecule to another. Hydrolases catalyze the hydrolytic cleavage of several bonds. Liases catalyze the cleavage of several bonds by means other than hydrolysis or oxidation, which means, for example, that they catalyze the removal of a group from or the addition of a group to a double bond, or other cleavages involving the rearrangement of electrons. Isomerases catalyze molecular rearrangement, which means changes within a molecule. Ligases catalyze the reactions in which two molecules bind. Some preferred enzymes according to the invention are oxidoreductases, which can act on different groups of donors, such as the CH-OH group, the aldehyde or oxo group, the CH-CH group, the CH-NH2 group, the CH group -NH, NADH or NADPH, nitrogen compounds, a sulfur group, a heme group, diphenols and related substances, hydrogen, simple donors with the incorporation of molecular oxygen, pairs of donors with the incorporation or reduction of molecular oxygen or others. Oxidoreductases can also act on the CH2 or X-H and Y-H groups to form an X-Y bond. 52-372 Typically, the enzymes belonging to the group of oxidoreductases can be referred to as oxidases, oxygenases, hydrogenases, dehydrogenases, reductases or the like. Specific examples of oxidoreductases comprise oxidases such as malate oxidase, glucose oxidase, hexose oxidase, aryl alcohol oxidase, alcohol oxidase, long chain alcohol oxidase, glycerol-3-phosphate oxidase, polyvinyl alcohol oxidase, D-arabinone-1, 4-lactone oxidase, D-mannitol oxidase, xylitol oxidase, oxalate oxidase, carbon monoxide oxidase, 4-hydroxyphenylpyruvate oxidase, dihydrouracil oxidase, ethanolamine oxidase, L-aspartate oxidase, sarcosine oxidase, urate oxidase, metantiol oxidase, 3-hydroxyanthranilate oxidase , laccase, catalase, fatty acid peroxidase, peroxidase, diarylpropan peroxidase, ferroxidase, pteridine oxidase, columbamine oxidase and the like. Additional specific examples of the oxidoreductases comprise oxygenases such as catechol 1,2-dioxygenase, gentisate 1,2-dioxygenase, homogentisate 1,2-dioxygenase, lipoxygenase, ascorbate 2,3-dioxygenase, 3-carboxyethylcatechol 2, 3- dioxygenase, indole 2, 3-dioxygenase, cafeate 3, -diioxygenase, arachidonate 5-lipoxygenase, biphenyl-2,3-diol 1,2-dioxygenase, linoleate 52-372 11-lipoxygenase, enzyme that cleaves acetylacetone, lactate 2-monooxygenase, phenylalanine 2-monooxygenase, inositol oxygenase and the like. Additional specific examples of the oxidoreductases comprise dehydrogenases such as alcohol dehydrogenase, glycerol dehydrogenase, propandiol phosphate dehydrogenase, L-lactate dehydrogenase, D-lactate dehydrogenase, glycerate dehydrogenase, glucose 1-dehydrogenase, galactose 1-dehydrogenase, allyl alcohol dehydrogenase, 4-hydroxybutyrate dehydrogenase, octanol dehydrogenase, aryl alcohol dehydrogenase, cyclopentanol dehydrogenase, long chain 3-hydroxyacyl-dehydrogenase, L-lactate dehydrogenase, D-lactate dehydrogenase, butanal dehydrogenase, 1, 2-cis-dihydrodiol dehydrogenase terephthalate , succinate dehydrogenase, glutamate dehydrogenase, glycine dehydrogenase, acid dehydrogenase, 4-cresol dehydrogenase, phosphonate dehydrogenase and the like. Specific examples of the reductases belonging to the group of oxidoreductases comprise enzymes such as diethyl reductase 2-methyl-3-oxosuccinate, tropinone reductase, long-chain acyl-CoA reductase, carboxylate reductase, D-proline reductase, glycine reductase and the like. 52-372 Other preferred enzymes according to the invention are the lyases, which can belong to any of the following groups: carbon-carbon lyases, carbon-oxygen lyases, carbon-nitrogen lyases, carbon-sulfur lyases, carbon-halide lyases, phosphorus- oxygen lyases and other lyases. Among the carbon-carbon lyases are the carboxy-liases, aldehyde-liases, oxo-acid-liases and others. Some specific examples belonging to these groups are oxalate decarboxylases, acetolactate decarboxylases, aspartate 4-decarboxylases, lysine decarboxylases, L-amino acid aromatic decarboxylases, methylmalonyl-CoA decarboxylases, carnitine decarboxylases, indole-3-glycerol-phosphate synthase, gallate decarboxylases, - branched chain oxo acid decarboxylases, tartrate decarboxylases, arylmalonate decarboxylases, fructose-bisphosphate aldolase, 2-dehydro-3-deoxy-phosphogluconate aldolase, trimethylamine aldolase oxide, propioin synthase, lactate aldolase, vanillin synthase, isocitrate lyase, hydroxymethylglutaryl-CoA lyase , 3-hydroxyapartate aldolase, tryptophanase, deoxyribodipyrimidine fotoliase, octadecanal decarbonylase and the like. Among the carbon-oxygen lyases are the hydroliases, lyases that act on the polysaccharides, 52-372 phosphates and others. Some specific examples are carbonate dehydratase, fumarate hydratase, aconite hydratase, citrate dehydratase, arabinonate dehydratase, galactonate dehydratase, altronate dehydratase, mannate dehydratase, dihydroxy acid dehydratase, 3-dehydroquinate dehydratase, propandiol dehydratase, glycerol dehydratase, maleate hydratase, oleate hydratase, pectate lyase, poly (β-D-mannuronate) lyase, oligogalacturonide lyase, poly (α-guluronate) lyase, xantanliase, ethanolamine phosphate phosphorylase, carboxymethyloxysuccinate lyase and others. Among the carbon-nitrogen lyases are the ammonia-liases, lyases that act on the amides, amidines, etc., amine-lyases and others. Specific examples of these groups of liases are aspartate ammonium lyase, phenylalanine ammonium lyase, ethanolamine ammonium lyase, glucosaminate ammonium lyase, argininosuccinate lyase, adenylosuccinate lyase, ureidoglycolate lyase, 3-ketovalidoxylamine C-N-lyase. Among the carbon-sulfur lyases, some specific examples are such as dimethylpropiotetin detiomethylase, aliin lyase, lactoylglutathione lyase and cysteine lyase. Among the carbon halide lyases, some specific examples are such as 3-chloro-D-alanine 52-372 dehydrochlorinase or dichloromethane dehalogenase. Among the phosphorus-oxygen lyases, some specific examples are such as adenylate cyclase, cycidylate cyclase, glycosylphosphatidylinositol diacylglycerol lyase. In the most preferred embodiments of the invention, the enzymes applied are the hydrolases comprising the glycosylases, enzymes acting on the acid anhydrides and enzymes acting on specific bonds such as ester bonds, ether bonds, carbon-nitrogen bonds, peptide bonds , carbon-carbon bonds, halide bonds, phosphorus-nitrogen bonds, sulfur-nitrogen bonds, carbon-phosphorus bonds, sulfur-sulfur bonds or carbon-sulfur bonds. Among the glycosylases, the preferred enzymes are the glucosidases, which are capable of hydrolyzing the O and S-glucosyl compounds or the N-glucosyl compounds. Some examples of glycosylases are α-amylase, β-amylase, glucan 1,4-a-glucosidase, cellulase, endo-1,3 (4) -β-glucanase, inulinase, endo-1,4-β-xylanase , oligo-1, 6-glucosidase, dextranase, chitinase, polygalacturonase, lysozyme, levanase, quercitrinase, galacturan 1,4-a-galacturonidase, isoamylase, glucan 1,6-a-glucosidase, glucan endo-1, 2-β- glucosidase, licheninase, agarase, exo-poly-a-galacturonosidase, K-carrageenase, 52-372 steril-ß-glucosidase, ß-glucosidase-strictosidine, mannosyl-oligosaccharide glucosidase, lactase, oligoxylglucan ß-glucosidase, polymannuronate hydrolase, chitosanase, poly (ADP-ribose) glucohydrolase, purine nucleosidase, inosine nucleosidase, uridine nucleosidase, adenosine nucleosidase and others. Among the enzymes that act on the acid anhydrides are, for example, those that act on the anhydrides containing phosphorus or sulfonyl. Examples of the enzymes that act on acid anhydrides are inorganic diphosphatase, trimetaphosphatase, adenosine triphosphatase, apyrase, nucleoside diphosphatase, acyl phosphatase, nucleotide diphosphatase, endopolyphosphatase, exopolyphosphatase, nucleoside phosphoacylhydrolase, triphosphatase, CDP-diacylglycerol diphosphatase, undecaprenyl diphosphatase , doliquildiphosphatase, oligosaccharide diphospholpoly diphosphatase, G-protein heterotrimeric GTPase, small monomeric GTPase, dinamin GTPase, tubulin GTPase, diphosphoinositol-polyphosphate diphosphatase, ATPase exporting H +, ATPase transporting monosaccharides, ATPase transporting maltose, ATPase carrying glycerol-3 phosphate, ATPase that transports oligopeptide, ATPase that transports polyamine, ATPase that transports peptides, ATPase that transports acyl-CoA fatty, ATPase that secretes protein and others. 52-372 The most preferred enzymes of the present invention are those which act on the ester linkages, among which are the carboxylic ester hydrolases, thiolyester hydrolases, phosphoric ester hydrolases, sulfuric ester hydrolases and the ribonucleases. Some examples of the enzymes acting on the ester bonds are acetyl-CoA hydrolase, palmitoyl-CoA hydrolase, succinyl CoA hydrolase, 3-hydroxyisobutyryl-CoA hydrolase, hydroxymethylglutaryl-CoA hydrolase, hydroxycylglutathione hydrolase, glutathione thiolesterase, formyl-CoA hydrolase, acetoacetyl-CoA hydrolase, S-formylglutathione hydrolase, S-succinyl-glutathione hydrolase, oleoyl- [acyl carrier protein] hydrolase, ubiquitin thiolesterase, [citrate- (pro-3S) -liase] thiolesterase, (S) -methylmalonyl-CoA Hydrolase, ADP-dependent short chain acyl-CoA hydrolase, ADP-dependent medium chain acyl-CoA hydrolase, acyl-CoA hydrolase, dodecanoyl- [acyl carrier protein] hydrolase, palmitoyl- (protein) hydrolase, 4-hydroxybenzoyl- CoA thioesterase, 2- (2-hydroxy-phenyl) -benzenesulfinate hydrolase, alkaline phosphatase, acid phosphatase, phosphoserine phosphatase, phosphatidate phosphatase, 5'-nucleotidase, 3'-nucleotidase, 3 '(2'), 5'-bisphosphate nucleotidase, 3-phytase, glucose-6-phosphatase, glycerol-2-phosphatase, phosphoglycerate phosphatase, glycerol-1-phosphatase, mannitol-1-phosphatase, sugar-phosphatase, sucrose- 52-372 phosphatase, inositol-1 (or 4) -monophosphatase, 4-phytase, phosphatidylglycerophosphatase, ADP phosphoglycerate phosphatase, N-acylneuraminate-9-phosphatase, nucleotidase, 3'-phosphatase polynucleotide, [glucogen-synthase-D] phosphatase, [ pyruvate dehydrogenase (lipoamide)] -phosphatase, [acetyl-CoA carboxylase] -phosphatase, 3-deoxy-human-octulosonate-8-phosphatase, 5'-phosphatase polynucleotide, terminal sugar-phosphatase, alkylacetylglycerophosphatase, 2-deoxyglucose-6-phosphatase , glucosylglycerol 3-phosphatase, 5-phytase, phosphodiesterase I, phosphodiesterase glycerophosphocholine, phospholipase C, phospholipase D, phospholipase phosphoinositide C, esfingomielin phosphodiesterase colinfosfodiesterasa glycerophosphocholine, phosphodiesterase alquilglicerofosfoetanolamina, glicerofosfodiesterasa glycerophosphoinositol, arylsulfatase esterilsulfatasa, glucosulfatasa, colinsulfatasa, cellulose-polisulfatasa, monomethyl sulfatase, D-lactate-2-sulphatase, glucuronate-2-sulphatase, prenyl diphosphatase, aryldialkyl phosphatase, diis opropyl-fluorophosphatase, oligonucleotidase, poly (A) -specific ribonuclease, yeast ribonuclease, deoxyribonuclease (pyrimidine dimer), Physarum polycephalum ribonuclease, alpha ribonuclease, Aspergillus nuclease Si, Serratia marcescens nuclease and more. The most preferred enzymes acting on the ester linkages are the carboxylic ester hydrolases such 52-372 such as carboxylesterase, arylesterase, triacylglycerol lipase, phospholipase A2, lysophospholipase, acetylesterase, acetylcholinesterase, cholinesterase, tropinesterase, pectinesterase, sterol esterase, chlorophyllase, L-arabinonolactonase, gluconolactonase, uronolactonase, stannases, retinyl-palmitate esterase, hydroxybutyrate dimer , hydrolase, acylglycerol lipase, 3-oxoadipate enol-lactonase, 1,4-lactonase, galactolipase, 4-pyridoxolactonase, acylcarnitine hydrolase, aminoacyl-tRNA hydrolase, D-arabinonolactonase, 6-phosphogluconolactonase, phospholipase Ai, 6-acetylglucose deacetylase, lipoprotein lipase, dihydrocoumarin hydrolase, limonin-D-anular-lactonase, spheroid lactonase, triacetate lactonase, actinomycin lactonase, orselinate-depside hydrolase, cephalosporin-C deacetylase, chlorogenate hydrolase, a-amino acid, esterase, 4-methyloxaloacetate esterase, carboxymethylenebutenolidase, deoxylimonate ring A lactonase, l-alkyl-2-acetylglycerophosphocholine esterase, fusarin ina-C or nitinesterase, sinapin esterase, wax hydrolase ester, phorbol-diester hydrolase, phosphatidylinositol deacylase, sialate O-acetylesterase, acetoxybutynyl biphi deacetylase, acetylsalicylate deacetylase, methylumbelliferyl acetate deacetylase, 2-piron-4,6-dicarboxylate lactonase, N -acetylgalactosaminoglycan deacetylase, esterase of the 52-372 juvenile hormone, bis (2-ethylhexyl) phthalate esterase, glutamate protein, methylesterase, 11-cis-retinyl-palmitate hydrolase, all-trans-retinyl-palmitate hydrolase, L-rhamnono-1,4-lactonase, 5- (3, 4-diacetoxybutyl-l-ynyl) -2,2'-bitioden deacetylase, fatty acyl ethyl ester synthase, xylono-1,4-lactonase, cetraxate benzylterase, acetylalkylglycerolacetylhydrolase, acetylxylan esterase, feruloyl esterase, cutinase, poly (3) -hydroxybutyrate) depolymerase, poly (3-hydroxyoctanoate) depolymerase, acyloxyacyl hydrolase, acyloxyacyl hydrolase, polyneuridine-aldehyde esterase and others. Accordingly, the enzymes acting on the ether linkages include the trialkylsulfonium hydrolases and the ether hydrolases. The enzymes that act on the ether bonds can act both on the thioether bonds and on the oxygen equivalent. Examples of specific enzymes belonging to these groups are adenosylhomocysteinase, adenosylmethionine hydrolase, isocorismatase, alkenylglycerophosphocholine hydrolase, epoxide hydrolase, trans-epoxysuccinate hydrolase, alkenylglycerophosphoethanolamine hydrolase, leukotriene-A hydrolase, hepoxylin-epoxide hydrolase and limonene-1, 2 -ephoxide hydrolase. Among the enzymes that act on the carbon-nitrogen bonds are the linear amides, the cyclic amides, the linear amidines, the cyclic amidines, the nitriles and other compounds. Specific examples belonging to these groups are asparaginase, glutaminase, α-amidase, amidase, urease, β-ureidopropionase, arylformamide, biotinidase, aryl acylamidase, amino acylase, aspartoacylase, acetylornithine deacetylase, acyl-lysine deacylase, succinyl- diaminopimelate, desuccinylase, pantotenase, ceramidase, coloilglycine hydrolase, N-acetylglucosamine-6-phosphate deacetylase, N-acetylmuramoyl-L-alanine amidase, 2- (acetamidomethylene) succinate hydrolase, 5-aminopentanamidase, formylmethionine deformylase, hippurate hydrolase, N-acetylglucosamine deacetylase , D-glutaminase, N-methyl-2-oxoglutastate hydrolase, glutamine- (asparagin) asa, alkylamidase, acilagmatine amidase, quitin deacetylase, peptidyl-glutaminase, N-carbamoyl-sarcosine amidase, N- (long-chain acyl) ethanolamine deacylase , Mimosinase, Acetyl-Putrescine Deacetylase, 4-Acetamidobutyrate Deacetylase, Theanine Hydrolase, 2- (Hydroxymethyl) -3- (Acetamidomethylene) Succinate Hydrolase, 4-Methylene Utaminase, N-formylglutamate deformylase, glucosphingolipid deacylase, aculeacin-A deacylase, peptide deformylase, dihydropyrimidinase, dihydroorotase, carboxymethyl-hydantoinase, creatininase, L-lysine-lactamase, arginase, guanidineacetase, creatinease, allantoic acid, 52-372 cytosine deaminase, riboflavinase, thiaminase, 1-aminocyclo-propan-1-carboxylate deamine and more. Some preferred enzymes of the present invention belong to the group of enzymes that act on the peptide bonds, a group which is also referred to as the peptidases. The peptidases can be further divided into exopeptidases, which act only close to a terminus of a polypeptide chain and the endopeptidases that act internally in the polypeptide chains. Enzymes that act on peptide bonds include enzymes selected from the group of aminopeptidases, dipeptidases, di-ortripeptidyl-peptidases, peptidyl-dipeptidases, carboxypeptidases of the serine type, metallocarboxypeptidases, carboxypeptidases of the cysteine type, omega peptidases, serine endopeptidases, cysteine endopeptidases, endopeptidases Aspartics, metalloendopeptidases and threonine endopeptidases. Some specific examples of the enzymes belonging to these groups are arecystinyl aminopeptidase, aminopeptidase peptide, prolyl aminopeptidase, arginyl aminopeptidase, glutamyl aminopeptidase, cytosol alanyl aminopeptidase, lysyl aminopeptidase, Met-X dipeptidase, non-stereospecific dipeptidase, non-specific cytosol dipeptidase, membrane dipeptidase , dipeptidase E, dipeptidyl-peptidase I, dipeptidyl-dipeptidase, tripeptidyl-peptidase I, tripeptidyl-peptidase II, X-Pro dipeptidyl-peptidase, peptidyl-dipeptidase A, Pro-X lysosomal carboxypeptidase, carboxypeptidase C, acylaminoacyl-peptidase, peptidyl-glucinamidase, (3-aspartyl-peptidase, ubiquitinyl hydrolase 1 , chymotrypsin, chymotrypsin C, metridine, trypsin, thrombin, plasmin, enteropeptidase, acro-sin, a-Lytic endopeptidase, glutamyl endopeptidase, cathepsin G, cucumisin, prolyl oligopeptidase, brachyurin, kallikrein in plasma, kallikrein in tissue, pancreatic elastase, elastase of leukocytes, chymase, cerevisin, hypodermin C, lysyl endopeptidase, endopeptidase La,? -renine, venombine AB, leucyl endopeptidase, tryptase, escutellarin, kexin, subtilisin, orycin, endopeptidase K, thermomicoline, termitase, endopeptidase So, activator plasminogen t, protein C (activated), pancreatic endopeptidase E, pancreatic elastase II, serine endopeptidase specific IgA, plasminogen activator u, venombine A, furine, myeloblastine, semenogelase, granzyme A, granzyme B, streptogrisin A, etreptogrisin B, glutamyl endopeptidase II, oligopeptidase B, omptin, togavirin, flavivirine, endopeptidase Clp, proprotein convertase 1, proprotein convertase 2, lactocepin, assemble, hepacivirine, espermosina, pseudomonalisina, xantomonalisina, peptidasa that processes the term C, 52-372 fisarolysin, cathepsin B, papain, ficaine, chemopapain, asclepain, clostripain, streptopain, actinidaine, cathepsin L, cathepsin H, cathepsin T, glycyl endopeptidase, cancer procoagulant, cathepsin S, picornain 3C, picornain 2A, caricaine, ananaine , stem bromelain, fruit bromelain, legume, histolysine, caspase-1, gingipain R, cathepsin K, adenain, bleomycin hydrolase, cathepsin F, cathepsin 0, cathepsin V, nuclear inclusion endopeptidase a, proteinase of the auxiliary component, L- peptidase, gingipain K, stafopain, separase, endopeptidase V-cath, cruzipain, calpain-1, calpain-2, pepsin A, pepsin B, gastricsin, chemosin, cathepsin D, nepentesin, renin, enzyme that converts proopiomelanocortin, aspergilopepsin I, Aspergillopepsin II, penicillopepsin, rhizopuspepsin, endotiapepsin, mucorpepsin, candidapepsia, sacaropepsin, rhodotorulapepsin, acrocylindropepsin, polyperopepsin, pyc-noporopepsin, esci talidopepsin A, escitalidopepsin B, cathepsin E, barrierpepsin, peptidase II signal, plasmepsin I, plasmepsin II, phytapsin, yapsin 1, thermopsin, prepilin peptidase, nodavirus endopeptidase, memapsin 1, memapsin 2, atrolisin A, microbial collagenase, leucolysin, stromelysin 1, meprin A, procollagen C-endopeptidase, astazin, pseudolysin, thermolysin, bacilolysin, 52-372 aureolysin, cocolysin, micolysin, gelatinase B, leishmanolysin, saccharolysin, gametolysin, serralisin, horrilisin, hulelisin, botropasin, oligopeptidase A, enzyme that converts endothelin, endopeptidase AD-AM10 and others. Suitable enzymes that act on the carbon-carbon bonds that can be found in ketone substances include, but are not limited to, oxaloacetase, fumarilacetoacetase, kynureninase, floretin hydrolase, acylpiruvate hydrolase, acetylpiruvate hydrolase, beta-diketone hydrolase, 2,6-dioxo -6-phenylhexa-3-enoate hydrolase, 2-hydroxyuconate-semialdehyde hydrolase and cyclohexane-1,3-dione hydrolase. Examples of enzymes within the group acting on the halide linkages are alkylalkidase, 2-haloacid dehalogenase, haloacetate dehalogenase, thyroxine deiodinase, haloalkane dehalogenase, 4-chlorobenzoate dedhalogenase, 4-chlorobenzoyl-CoA dehalogenase, atrazine chlorohydrolase and the like. Additional examples according to the present invention of enzymes that act on specific bonds are phosphoamidase, N-sulfoglucosamine sulfohydrolase, cyclamate sulfohydrolase, phosphonoacetaldehyde hydrolase, phosphonoacetate hydrolase, trithionate hydrolase, UDPsulfoquinovosa synthase and 52-372 similar. According to the present invention, the enzymes added in the biodegradable chewing gum may be of a single type or of different types in combination. Some enzymes require cofactors to be effective. Examples of such cofactors are 5,10-methenyl tetrahydrofolate, ammonium, ascorbate, ATP, bicarbonate, bile salts, biotin, cofactor of bis (molibdopterin guanin dinucleotide) olibdene, cadmium, calcium, cobalamin, cobalt, coenzyme F430, coenzyme-A, copper, dipyrromethane, dithiothreitol, divalent cation, FAD, flavin, flavoprotein, FMN, glutathione, heme, hemetiolate, iron, iron (2+), iron-molybdenum, iron-sulfur, lipoyl group, magnesium, manganese, metal ions, molybdenum , molybdopterin, monovalent cation, NAD, NAD (P) H, nickel, potassium, PQQ, protoheme IX, pyridoxal-phosphate, pyruvate, selenium, siroheme, sodium, tetrahydropteridine, thiamine diphosphate, topaquinone, tryptophan triptofilquinone (TTQ), tungsten , vanadium and zinc. In accordance with the general principles of manufacture, one embodiment within the scope of the invention, several different suitable ingredients are listed and explained below. The chewing gum according to the invention may comprise coloring agents. According to one 52-372 embodiment of the invention, the chewing gum may comprise coloring and bleaching agents such as FD &; C and lacquers, fruit and vegetable extracts, titanium dioxide and combinations thereof. Additional components of the base for chewing gum include antioxidants, for example, butylated hydroxytoluene (BHT), butylated hydroxyanisole (BHA), propyl gallate and tocopherols and preservatives. In one embodiment of the invention, the chewing gum comprises softeners in an amount of about 0 to about 18% by weight of the chewing gum, more typically from about 0 to about 12% by weight of the chewing gum. According to the invention, softeners / emulsifiers can be added to the chewing gum and to the gum base. A base formulation for gum may, according to the present invention, comprise one or more softening agents, for example, sucrose polyesters, including those described in WO 00/25598, which is incorporated herein by reference, tallow, tallow hydrogenated, hydrogenated and partially hydrogenated vegetable oils, cocoa butter, glycerol monostearate, glycerol triacetate, lecithin, mono, di and triglycerides, acetylated monoglycerides, fatty acids (for example, 52-372 stearic, palmitic, oleic and linoleic acids) and combinations thereof. As used herein, the term "softener" designates an ingredient, which softens the base for gum or the chewing gum formulation, and encompasses waxes, fats, oils, emulsifiers, surfactants and solubilizers. To further soften the rubber base and provide it with water binding properties, which give the rubber base a nice smooth surface and reduce its adhesive properties, usually one or more emulsifiers are added to the composition, typically in an amount of 0. to 18% by weight, preferably, from 0 to 12% by weight of the gum base. Monkeys and diglycerides of edible fatty acids, esters of lactic acid and acetic acid esters of mono and diglycerides of edible fatty acids, acetylated mono and diglycerides, sugar esters of edible fatty acids, stearates of Na, K, Mg and Ca, lecithin, hydroxylated lecithin and the like are examples of emulsifiers conventionally used, which can be added to the base for chewing gum. In the case of the presence of a biological or pharmaceutically active ingredient as defined below, the formulation may comprise certain emulsifiers and / or solubilizers in order to improve the dispersion and release the ingredient 52-372 active. Waxes and greases are conventionally used for the adjustment of the consistency and for softening the base for chewing gum when preparing the bases for chewing gum. In relation to the present invention, any type of conventionally used and suitable wax and fat can be used, such as, for example, rice bran wax, polyethylene wax, petroleum wax (refined paraffin and microcrystalline wax), paraffin wax, bees, carnauba wax, candelilla wax, cocoa butter, defatted cocoa powder and any suitable oil or fat, such as partially hydrogenated vegetable oils or partially hydrogenated animal fats. In one embodiment of the invention, the chewing gum comprises a filler. A base formulation for chewing gum may, if desired, include one or more fillers / texturizers, including as examples, magnesium and calcium carbonate, sodium sulfate, crushed lime, silicate compounds such as magnesium silicate and aluminum, kaolin and clay, aluminum oxide, silicon oxide, talc, titanium oxide, mono, di and tricalcium phosphates, cellulose polymers, such as wood and combinations thereof. 52-372 In one embodiment of the invention, the chewing gum comprises a filling in an amount of from about 0 to about 50% by weight of the chewing gum, more typically from about 10 to about 40% by weight of the gum chew In the present context, the ingredients of the chewing gum may comprise, for example, bulk sweeteners, high intensity sweeteners, flavoring agents, softeners, emulsifiers, coloring agents, binding agents, acidulants, fillers, antioxidants and other components such as pharmaceutically or biologically active substances, which confer the desired properties to the finished product of the chewing gum. Suitable bulk sweeteners include both sugar sweetener and non-sugar sweetener components. Bulk sweeteners typically constitute from about 5 to about 95% by weight of the chewing gum, more typically from about 20 to about 80% by weight, such as from 30 to 60% by weight of the gum. Useful sugar sweeteners are saccharide-containing components, commonly known in the field of chewing gums include, but are not limited to, sucrose, dextrose, maltose, dextrins, trehalose, D- 52-372 tagatose, dry invert sugar, fructose, levulose, galactose, corn syrup solids and the like, alone or in combination. Sorbitol can be used as a non-sugar sweetener. Other sweeteners that are not useful sugar include, non-exclusively, other sugar alcohols, such as mannitol, xylitol, hydrogenated starch hydrolysates, maltitol, isomaltol, erythritol, lactitol and the like, alone or in combination. The high intensity artificial sweetening agents can also be used alone or in combination with the above sweeteners. Preferred high intensity sweeteners include, but are not limited to, sucralose, aspartame, salts of acesulfame, alitame, saccharin and its salts, cyclamic acid and its salts, glycyrrhizin, dihydrochalcones, thaumatin, monelin, stereoside and the like, together or combination. In order to provide a perception of sweetness and flavor that lasts longer, it may be desirable to encapsulate or otherwise control the release of at least a portion of the artificial sweetener. Techniques such as wet granulation, wax granulation, spray drying, spray cooling, fluid bed coating, coacervation, encapsulation in yeast cells and fiber extrusion can be used to achieve 52-372 desired release characteristics. The encapsulation of the sweetening agents can also be provided using other components of the chewing gum, such as resinous compounds. The level of use of the artificial sweetener will vary considerably and will depend on such factors as the potency of the sweetener, the rate of release, the sweetness of the desired product, the level and type of flavor used, and cost considerations. Thus, the active level of artificial sweetener can vary from about 0.02 to about 30% by weight, preferably from 0.02 to about 8% by weight. When carriers used for encapsulation are included, the level of use of the encapsulated sweetener will be proportionally higher. Combinations of sugar sweeteners and / or non-sugar sweeteners can be used in the chewing gum formulation processed according to the invention. In addition, the softener may also provide additional sweetness such as with aqueous solutions of sugar or alditol. If a low-calorie gum is desired, a low-calorie bulk agent can be used. Examples of low-calorie bulk agents include polydextrose, Raftilose, Raftiline, fructooligosaccharides (NutraFlora®), palatinose oligosaccharides; hydrolyzed 52-372 guar gum (for example, Sun Fiber®) or non-digestible dextrins (for example, Fibersol®). However, other low-calorie bulk agents can be used. The chewing gum according to the present invention may contain aromatics and flavoring agents including natural and synthetic flavors, for example, in the form of natural plant components, essential oils, essences, extracts, powders, including acids and other substances capable to affect the taste profile. Examples of liquid and powdered flavorings include coconut, coffee, chocolate, vanilla, grapefruit, orange, lime, mint, licorice, caramel aroma, honey flavor, peanut, walnut, cashew, hazelnut, almond, pineapple, strawberry, raspberry , tropical fruits, cherries, cinnamon, peppermint, wintergreen, spearmint, eucalyptus and mint, fruit essences such as apple, pear, peach, strawberry, apricot, raspberry, cherry, pineapple and plum. The essential oils include peppermint, spearmint, menthol, eucalyptus, clove oil, bay oil, anise, thyme, cedar leaf oil, nutmeg and oils from the fruits mentioned above. The flavor of the chewing gum can be a natural flavoring agent, which is freeze dried, preferably in the form of a powder, slices or 52-372 pieces or combinations thereof. The particle size may be less than 3 mm, less than 2 mm or more preferably less than 1 mm, calculated as the longest dimension of the particle. The natural flavoring agent may also be in a form in which the particle size is from about 3 μm to 2 mm, such as from 4 μm to 1 mm. Preferred natural flavoring agents include seeds of a fruit, for example, strawberry, blackberry and raspberry. Various synthetic flavors, such as a flavor of mixed fruits, can also be used in the centers of the chewing gum present. As indicated above, the aromatic agent can be used in smaller amounts than those conventionally used. The aromatic and / or flavoring agents may be used in an amount of about 0.01 to about 30% by weight of the final product depending on the desired intensity of the flavor and / or flavor used. Preferably, the aroma / flavor content is in the range of about 0.2 to 3% by weight of the total composition. In one embodiment of the invention, the flavoring agents comprise natural and synthetic flavors in the form of natural plant components, essential oils, essences, extracts, powders, including acids 52-372 and other substances capable of affecting the flavor profile. The additional chewing gum ingredients, which may be included in the chewing gum according to the present invention, include surfactants and / or solubilizers, especially when pharmaceutically or biologically active ingredients are present. As examples of types of surfactants to be used as solubilizers in a chewing gum composition according to the invention, reference is made to HP Fiedler, Lexikon der Hilfstoffe für Pharmacie, Kosmetik und Angrenzende Gebiete, pages 63-64 (1981), and lists of approved emulsifiers for foods from individual countries. Anionic, cationic, amphoteric or non-ionic solubilizers can be used. Suitable solubilisers include lecithins, polyoxyethylene stearate, fatty acid esters of polyoxyethylene sorbitan, fatty acid salts, esters of mono and diacetyl tartaric acid of mono and diglycerides of edible fatty acids, citric acid esters of mono- and diglycerides of fatty acids edible, sucrose esters of fatty acids, polyglycerol esters of fatty acids, polyglycerol esters of acid interesterified castor oil (E476), estearoillatilato sodium, sodium lauryl sulfate and sorbitan esters of fatty acids and hydrogenated castor oil polyoxyethylated (for example, the product 52-372 sold under the trade name CREMOPHOR), block copolymers of ethylene oxide and propylene oxide (e.g. products sold under trade names PLURONIC and the POLOXAMER), polyoxyethylene fatty alcohol ethers, fatty acid esters, polyoxyethylene sorbitan, sorbitan esters of fatty acids and esters of polyoxyethylene stearic acid. Particularly suitable solubilizers are polyoxyethylene stearates, such as, for example, polyoxyethylene stearate (8) and polyoxyethylene stearate (40), the polyoxyethylene sorbitan fatty acid esters sold under the trade name TWEEN, for example TWEEN 20 (monolaurate), TWEEN 80 (Monooleate), TWEEN 40 (monopalmitate), TWEEN 60 (monostearate) or TWEEN 65 (tristearate), esters of mono- and diacetyl tartaric acid of mono and diglycerides of edible fatty acids, citric acid esters of mono- and diglycerides of edible fatty acids , sodium stearoylactylate, sodium lauryl sulfate, polyoxyethylated hydrogenated castor oil, block copolymers of ethylene oxide and propylene oxide and polyoxyethylene fatty alcohol ether. The solubilizer can be a single compound or a combination of several compounds. In the presence of an active ingredient, the chewing gum can also comprise in a 52-372 preferred, a carrier known in the art. In one embodiment, the chewing gum of the invention comprises a pharmaceutical, cosmetic or biologically active substance. Examples of such active substances, an extensive list of which is found, for example, in WO 00/25598, which is incorporated herein by reference, includes drugs, dietary supplements, antiseptic agents, pH adjusting agents, anti-smoking agents and substances for the care or treatment of the oral cavity and teeth, such as hydrogen peroxide and compounds capable of releasing urea during chewing. Examples of useful active substances in the form of antiseptics include salts and derivatives of guanidine and biguanidine (for instance chlorhexidine diacetate) and the following types of substances with limited water-solubility: quaternary ammonium compounds (e.g. ceramine, chloroxylenol, methyl violet, chloramine), aldehydes (e.g. paraformaldehyde), derivatives of dequaline, polynoxyline, phenols (e.g. thymol, p-chlorophenol, cresol), hexachlorophene, compounds salicylic of anilide, triclosan, halogenes (iodine, iodophors, chloroamine, salts of dichlorocyanuric acid), alcohols (3,4-dichlorobenzyl alcohol, benzyl alcohol, phenoxyethanol, phenylethanol), see also, Martindale, The Extra 52-372 Pharmacopoeia, 28th edition, pages 547-578; metal salts, complexes and compounds with limited water solubility, such as aluminum salts (for example potassium sulfate and aluminum A1K (S0) 2, 12H20) and must include salts, complexes and compounds of boron, barium, strontium, iron, calcium, zinc, (zinc acetate, zinc chloride, zinc gluconate), copper (copper chloride, copper sulfate), lead, silver magnesium, sodium, potassium, lithium, molybdenum, vanadium; other compositions for the care of the mouth and teeth: for example; salts, complexes and compounds containing fluorine (such as sodium fluoride, sodium monofluorophosphate, aminofluorides, stannous fluoride), phosphates, carbonates and selenium. Additional active substances can be found in J. Dent. Res. Vol. 28 No. 2, pages 160-171, 1949. Examples of active substances in the form of agents that adjust the pH in the oral cavity include: acids, such as adipic acid, succinic acid, fumaric acid or salts thereof or salts of citric acid, tartaric acid, malic acid, acetic acid, lactic acid, phosphoric acid and glutaric acid and acceptable bases, such as carbonates, acid carbonates, phosphates, sulfates or oxides of sodium, potassium, ammonium, magnesium or calcium, especially magnesium and calcium. The active ingredients may comprise the 52-372 compounds mentioned below or derivatives thereof, but are not limited thereto: Acetaminophen, Acetylsalicylic, Buprenorphine, Bromhexine, Celcoxib, Codeine, Diphenhydramine, Diclofenac, Etoricoxib, Ibuprofen, Indomethacin, Ketoprofen, Lumiracoxib, Morphine, Naproxen , Oxicodon, Parecoxib, Piroxicam, Pseudoephedrine, Rofecoxib, Tenoxicam, Tramadol, Valdecoxib, Calcium carbonate, Magaldrate, Disulfiram, Bupropion, Nicotine, Acitromycin, Clarithromycin, Clotrimazole, Erythromycin, Tetracycline, Granisetron, Ondansetron, Promethazine, Tropisetron, Brompheniramine, Cetericin , Leco-Cetericin, Chlorocycline, Chlorpheniramine, Chlorpheniramine, Diphenhydramine, Doxylamine, Fenofenadine, Guaifenesin, Loratidine, des-Loratidine, Phenyltoloxamine, Promethazine, Pyridamine, Terfenadine, Troxerutin, Methyldopa, Methylphenidate, Benzalkonium Chloride, Bencethonium Chloride, Cetylpyrid Chloride ., Chlorhexidine, Ecabet-sodium, Haloperidol, Allopurinol, Colchinin, Theophylline , Propanolol, Prednisolone, Prednisone, Fluoride, Urea, Miconazole, Actot, Glibenclamide, Glipizide, Metformin, Miglitol, Repaglinide, Rosiglitazone, Apomorphine, Cialis, Sildenafil, Vardenafil, Diphenoxylate, Simethicone, Cimetidine, Famotidine, Ranitidine, Ratinidine, Cetricin, Loratadine , Aspirin, Benzocaine, Dextromethorphan, Ephedrine, Phenylpropanola ina, Pseudoephedrine, Cisapride, 52-372 Domperidone, Metoclopramide, Acyclovir, Dioctyl Sulfosuccinate, Phenolphthalein, Almotriptan, Eletriptan, Ergotamine, Migea, Naratriptan, Rizatriptan, Sumatriptan, Zolmitriptan, aluminum salts, calcium salts, iron salts, silver salts, zinc salts , Amphotericin B, Chlorhexidine, Miconazole, Triamcinolonacetonide, Melatonin, Phenobarbitol, Caffeine, Benzodiazepine, Hydroxyzine, Meprobamate, Phenothiazine, Bucycin, Bromethamine, Cinnarcin, Cyclin, Diphenhydramine, Dimenhydrinate, Buflomedil, Amphetamine, Caffeine, Ephedrine, Orlistat, Phenylephedrine, Phenylpropanolamine, Pseudoephedrine, Sibutramine, Ketoconazole, Nitroglycerin, Nystatin, Progesterone, Testosterone, Vitamin B12, Vitamin C, Vitamin A, Vitamin D, Vitamin E, Pilocarpine, Aluminum Aminoacetate, Cimetidine, Esomeprazole, Famotidine, Lansoprazole, Magnesium Oxide, Nizatide and / or Ratinidine. Generally, it is preferred that the chewing gum and the gum bases prepared according to the invention are based solely on biodegradable polymers. However, within the scope of the invention elastomeric elastomers or plasticizers can be applied to conventional chewing gum. Thus, in one embodiment of the invention, the biodegradable polymer comprises at least 5% to at least 90% of the chewing gum polymers, and wherein the rest of the polymers comprise polymers generally considered non-biodegradable, such as natural resins, synthetic resins and / or synthetic elastomers. In one embodiment of the invention, the natural resins comprise terpene resins, e.g., derived from alpha-pinene, beta-pinene, and / or d-limonene, natural terpene resins, glycerol esters of gum rosins, rosins of talol, wood rosins or other derivatives thereof, such as glycerol esters of partially hydrogenated rosins, glycerol esters of partially polymerized rosins, glycerol esters of partially dimerized rosins, pentaerythritol esters of partially hydrogenated rosins, methyl esters of rosins , partially hydrogenated methyl esters of rosins and pentaerythritol esters of rosins and combinations thereof. In one embodiment of the invention, the synthetic resin comprises polyvinyl acetate, vinyl acetate-vinyl laurate copolymers and mixtures thereof. Generally within the scope of the invention, useful synthetic elastomers include, but are not limited to, the synthetic elastomers listed in 52-372 Food and Drug Administration, CFR, Title 21, Section 172,615, Chewable, Synthetic Substances), such as polyisobutylene, for example, having an average molecular weight by gas pressure chromatography (GPC) in the range of about 10,000 to about 1,000,000, including the range of 50,000 to 80,000, isobutylene-isoprene copolymer (butyl elastomer), styrene-butadiene copolymers, for example, having ratios from about 1: 3 to about 3: 1, polyvinyl (PVA), for example having an average molecular weight per GPC in the range of 2,000 to about 90,000, such as in the range of 3,000 to 80,000, including the range of 30,000 to 50,000, wherein the polyvinyl acetates with weight The highest molecular weight are typically used in a base for pump gum, polyisoprene, polyethylene, vinyl acetate-vinyl laurate copolymer, for example, which has a vinyl laurate emulsion of from about 5 to about 50% by weight, such as from 10 to 45% by weight of the copolymer, and combinations thereof. It is common in the industry to combine in a rubber base a synthetic elastomer having a high molecular weight and an elastomer with a low molecular weight. Presently preferred combinations of the synthetic elastomers include, but are not limited to, polyisobutylene and styrene-butadiene, polyisobutylene and polyisoprene, polyisobutylene and isobutylene-isoprene copolymer (butyl rubber) and a combination of polyisobutylene, styrene-butadiene copolymer and copolymer of isobutylene-isoprene, and all the above individual synthetic polymers, in admixture with polyvinyl acetate, vinyl acetate-vinyl laurate copolymers, respectively, and mixtures thereof. According to the invention, the chewing gum base components that are used herein may include one or more resinous compounds which contribute to obtain the chewable properties and act as plasticizers for the elastomers of the gum base composition. In the present context, plasticizers for elastomers include, but are not limited to, esters of natural rosin, often referred to as ester gums, including as examples, glycerol esters of partially hydrogenated rosins, glycerol esters of polymerized rosins, esters of glycerol of partially dimerized rosins, glycerol esters of tallow rosins, pentaerythritol esters of partially hydrogenated rosins, methyl esters of rosins, partially hydrogenated methyl esters of rosins and pentaerythritol esters of rosins. Other compounds 52-372 useful resins include synthetic resins such as terpene resins derived from alpha-pinene, beta-pinene, and / or d-limonene, natural terpene resins and any suitable combinations of the foregoing. The choice of plasticizers for elastomers will vary depending on the specific application and the type of elastomer used. The chewing gum according to the invention can be provided with an external coating. The applicable hard coating can be selected from the group comprising a sugar coating or one without sugar and a combination thereof. The hard coating may, for example, comprise 50 to 100% by weight of a polyol selected from the group consisting of sorbitol, maltitol, mannitol, xylitol, erythritol, lactitol and Isomait and variations thereof. In one embodiment of the invention, the outer coating is a film comprising at least one component selected from the group consisting of an agent that forms an edible film and a wax. The film forming agent can, for example, be selected from the groups comprising a cellulose derivative, a modified starch, a dextrin, gelatin, shellac, gum arabic, zein, a vegetable gum, a synthetic polymer and any combination of the same. In one embodiment of the invention, the external coating 52-372 comprises at least one additive component selected from the group comprising a binder, a moisture absorbing component, a film forming agent, a dispersing agent, an anti-adhesive component, a bulking agent, a flavoring agent, a coloring agent, a pharmaceutical or cosmetically active component, a lipid component, a wax component, a sugar, an acid and an agent capable of accelerating degradation after chewing of the degradable polymer. In a further embodiment of the invention, the outer coating is a smooth coating. The soft coating may comprise a sugar-free coating agent. Unless otherwise indicated, as used herein, the term "molecular weight" means the number average molecular weight (Mn) in g / mol. The short form PD designates polydispersity. In the same way, the weight of the enzymes is provided in kilodaltons, abbreviated kDa. The vitreous transition temperature (Tg) can be determined by, for example, DSC (DSC: differential scanning calorimetry). The DSC can be applied generally to determine and study the thermal transitions of a polymer and in a specific way, the technique can be applied for the determination of a second order transition of a material, that is, a transition 52-372 thermal that involves a change in heat capacity, but that has no latent heat. The vitreous transition is a transition of second order. The following non-limiting examples illustrate the manufacture of a chewing gum according to the invention.

EXAMPLE 1 Preparation of a Polyester Elastomer Obtained by Ring Opening Polymerization An elastomer sample was synthesized within a glove box with dry N2, as follows. In a 500 mL resin kettle, equipped with a mechanical stirrer in the upper part, 3.143 of pentaerythritol and 0.5752 g of Sn (Oct) 2 (2.0 mL of 1442 g of Sn (Oct) 2 2/5 mL in methylene chloride), under a purge of dry N2 gas. The methylene chloride was allowed to evaporate under the N2 purge for 15 minutes. Next, e-caprolactone (1144 g, 10 moles), trimethylene carbonate (31 g, 0.30 moles) and d-valerolactone (509 g, 5.1 moles) were added. The resin kettle was immersed in an oil bath at a constant temperature of 130 ° C and stirred for 13.9 hours. Subsequently, the cauldron was removed from the oil bath and allowed to cool to room temperature. The elastic solid product was removed in small pieces, 52-372 using a blade, and placed in a plastic container. The product characterization indicated Mn = 56,000 g / mol and Mw = 98,700 g / mol (gel permeation chromatography with an on-line MALLS detector) and a Tg = -58.9 ° C. (DSC, heating speed 10 ° C / minute).

EXAMPLE 2 Preparation of a Polyester Elastomer Obtained by Ring Opening Polymerization An elastomer sample was synthesized within a glove box with dry N2, as follows. In a 500 mL resin kettle, equipped with a mechanical stirrer in the upper part, 3.152 pentaerythritol and 0.5768 g Sn (0ct) 2 (2.0 mL of 1442 g Sn (Oct) 2 2/5 mL in methylene chloride), under a purge of dry N2 gas. The methylene chloride was allowed to evaporate under the N2 purge for 15 minutes. Next, e-caprolactone (1148 g, 10 moles), trimethylene carbonate (31 g, 0.30 moles) and d-valerolactone (511 g, 5.1 moles) were added. The resin pot was immersed in an oil bath at a constant temperature of 130 ° C and stirred for 13.4 hours. Subsequently, the cauldron was removed from the oil bath and allowed to cool to room temperature. The elastic solid product was removed in small pieces, 52-372 using a blade, and placed in a plastic container. The product characterization indicated Mn = 88,000 g / mol and Mw = 297,000 g / mol (gel permeation chromatography with an on-line MALLS detector) and a Tg = -59.4 ° C. (DSC, heating speed 10 ° C / minute).

EXAMPLE 3 Preparation of Polyester Resin Obtained by Ring Opening Polymerization A resin sample was produced using a 10 L cylindrical, jacketed, cylindrical experimental reactor equipped with a glass stirring bar and shaker blades. Teflon and with an outlet in the background. The heating of the reactor content was achieved by circulation of silicone oil, thermostated at 130 ° C, through the outer jacket. The e-caprolactone (358.87 g, 3.145 moles) and the 1,2-propylene glycol (79.87 g, 1050 moles) were charged to the reactor together with stannous octoate (1.79 g, 4.42 x 10-3 moles) as the catalyst and reacted approximately 30 minutes at 130 ° C. Next, molten D, L-lactide (4.877 kg, 33.84 mol) was added and the reaction continued for about 2 hours. At the end of this period, the bottom outlet was opened and the molten polymer was left 52-372 will be drained in a can of Teflon-coated paint. The product characterization indicated Mn = 6,000 g / mol and Mw = 7,000 g / mol (gel permeation chromatography with an on-line MALLS detector) and Tg = 25-30 ° C (DSC, heating rate 10 ° C / min. ).

EXAMPLE 4 Preparation of a Polyester Elastomer Obtained by Step Growth Polymerization An elastomer sample was produced using a 500 mL resin kettle equipped with a stirrer on top, a nitrogen gas inlet tube, thermometer and dome of distillation for the removal of methanol. 83.50 g (0.43 mol) of dimethyl terephthalate, 99.29 g (0.57 mol) of dimethyl adipate, 106.60 g (1.005 mol) of di (ethylene glycol) and 0.6 g of calcium acetate monohydrate are charged to the caldron. Under nitrogen, the mixture is heated slowly with stirring until all the components melt (120-140 ° C). The heating and stirring continue and the methanol is continuously distilled. The temperature rises slowly in the range of 150-200 ° C until the evolution of methanol ceases. The heating is stopped and the contents allowed to cool to approximately 100 ° C. The reactor cover is removed and the molten polymer is poured 52-372 carefully in a receiving container. The product characterization indicated Mn = 40,000 g / mol and Mw = 190,000 g / mol (gel permeation chromatography with an on-line MALLS detector) and a Tg = -30 ° C. (DSC, heating speed 10 ° C / minute).

EXAMPLE 5 Preparation of the gum bases The process for preparing the gum bases was carried out in the following manner. The elastomer and the resin are added to a mixing cauld provided with mixing means such as, for example, Z-shaped arms placed horizontally. The cauldron has been preheated for 15 minutes at a temperature of about 60-80 ° C. The mixture was mixed for 10-20 minutes until the entire mixture becomes homogeneous. The mixture is then discharged into the tundish and allowed to cool to room temperature from the discharge temperature of 60-80 ° C. Two different bases for rubber were prepared, as shown in table 1. 2-372 Table 1: Preparation of the base for gum.

EXAMPLE 6 Preparation of the chewing gum The gum bases of Example 5 were used in the preparation of the chewing gum with the basic formulations shown in Table 2. The formulations are identical, with the exception that substitutes are added. sorbitol enzyme in equivalent amounts. 52-372 Table 2: Chewing gum formulations with different concentrations of the enzyme. Peppermint flavor The concentrations of the ingredients are given in percent by weight.

The concentrations of the enzyme of 0.32, 0.8, 1.6, 4.8 and 14.4 that are in percent by weight of the total chewing gum formulation, correspond to 1.0, 2.5, 5.0, 15.0 and 45.0 percent, related to the content of the rubber base constituting 32 percent by weight of the chewing gum. Softeners, emulsifiers and fillers can be added alternately to the polymers as part of the rubber base preparation. The gum bases of Example 5 were used with the chewing gum formulations of Table 2 and the following chewing gum samples were prepared: 52-372 Table 3: Chewing gum samples with different bases for gum, enzyme concentrations and enzyme types.

As it appears from Table 3, each chewing gum sample was prepared with none or one of four different enzymes, which were added in different amounts. The samples without enzyme were prepared as references. Applied enzymes purchased from companies located in Denmark: Antra ApS (Bromelain, product name Bromelin), Novozymes (Neutrase and Trypsin, product names Neutrase 0.8 L and Trypsin Pancreatic Novo 6.0 S, Salt Free Type) and Danisco Cultor (Glucose oxidase, product name TS-E 760). The enzymes Bromelain, Neutrase and Glucose oxidase are available as powders and the enzyme Trypsin as a liquid. The products of the chewing gum were prepared 52-372 as follows: The gum base was added to a mixing cauld provided with mixing means, such as for example Z-shaped arms placed horizontally. The cauldron has been preheated for 15 minutes at a temperature of approximately 60-80 ° C or the chewing gum is made in a single step, immediately after the preparation of the rubber base in the same mixer, where the base for gum and the cauldron have a temperature of approximately 60-80 ° C. One half of the sorbitol portion was added together with the gum base and mixed for 3 minutes. Peppermint and menthol were added to the cauldron and mixed for 1 minute. Half of the remaining portion was added and mixed for 1 minute. The softeners are added slowly and mixed for 7 minutes. Next, aspartame and acesulfame are added to the cauldron and mixed for 3 minutes. Xylitol was added and mixed for 3 minutes. Finally, the enzyme is added and mixing continues for l-l ^ - = minutes. After the addition of the enzyme, care must be taken not to exceed the temperature, which is tolerated by the type of enzyme applied. The mixture of the resulting gum is then discharged and, for example, transferred to a tundish at a temperature of 40-48 ° C. The rubber is 52-372 rolls and cuts into cores, bars, spheres, cubes and any other desired shape, optionally followed by coating and polishing processes before packing or use. Obviously, within the scope of the invention, other processes and ingredients may be applied in the chewing gum manufacturing process, for example, the one-step method may be an indulgent alternative.

EXAMPLE 7 Degradation of the chewing gum The chewing gum products prepared according to example 5 were chewed in a chewing device (CF Jansson) and left for degradation either in air or in a phosphate buffer. The corresponding chew pieces without chewing were exposed to equivalent degradation. Both chewed and chewed pieces of gum were observed over a period of 10 days and degradation was evaluated based on visual rating and GC / MS analysis. The different types of chewing gum pieces according to Table 3 were exposed separately to the next experimental setup, where only points 4 and 6 are applied for the non-chewed pieces of gum. 1. Placed in a chewing device containing 20 ml of phosphate buffer solution 52-372 (0.012 M diacid ammonium phosphate, adjusted to pH 7.4 with a 2M NaOH solution). 2. Chewing for 5 minutes with a chewing frequency of 60 chews / minute. 3. Removal of the solution and formed in a sphere. 4. Placed in the center of a Petri dish, or placed in a closed beaker containing 5 ml (0.012 M) of phosphate buffer solution, adjusted to pH 5.6. 5. The petri dish is placed at 30 ° C at 70% relative humidity (RH), or the vessel containing the buffer solution is placed at 30 ° C. 6. Evaluated for degradation.

Evaluation procedures; Visual evaluation: The degradation of each piece of chewing gum was graded with two scales, which are explained below. The visual evaluation was carried out after 3, 6 and 10 days. The scale of 10 to 0 is related to the appearance of the pieces of chewing gum in air or in shock absorber: 10: No notable degradation. 9: Deviation from the initial form; so, the 52-372 piece of chewing gum is slightly open. 8: The piece of chewing gum is even more open and unfolds more. The onset of disintegration has also occurred. 7: Cracking of the surface of the rubber part begins. 5: The surface of the chewing gum is very cracked. 1: The piece of chewing gum is completely disintegrated and is in suspension. 0: The piece of chewing gum is completely degraded. The PI PÍO scale is related to the appearance of the buffer solution in which the pieces of chewing gum are placed: PO: No visible change in the solution. Pl: The solution appears transparent, although a few small particles have appeared. P3: The solution is relatively transparent, although it contains several small flakes and / or a few larger "gelatinous" particles. Q6: The solution is very "gelatinous", while the number and size of the flakes has increased and the transparency of the solution has decreased. PÍO: The solution contains the entire piece of rubber 52-372 chewing in the form of small particles.

GC / MS analysis: The method used in the evaluation by GC / MS included sampling in the upper space (Turbo Matrix 40 by Perkin Elmer), thus, both the chewing gum residues and the buffer solution after the degradation were placed in vials where the release of the components was obtained in the upper space. After a period of equilibrium a sample of the air from the upper space was injected into a GC / MS system (Clarus 500 by Perkin Elmer) and in the resulting chromatograms, the areas of the relevant peaks were evaluated, so the degradation of different Chewing gums were compared, as described in the next results section.

Results of the visual evaluation The results of the visual evaluation of the gum pieces containing the enzyme (and the reference gum piece without enzyme) left for degradation are provided here below. With respect to chewing gum, left in the air, the change, which could be detected visually, was minor. After 10 days, the unglazed rubber pieces were given a degradation rating of 10, while 52-372 that the chewed gum pieces were given a rating of 9 for the reason that their spherical shape was altered and a slight opening or splitting could be observed. With regard to the chewing gum left in the buffer solution, the effect of the enzyme was more pronounced. For both chewed and chewed gum, these experiments showed that chewing gum inclusion in some cases has an accelerating effect on the degradation of chewing gum.

Table 4: Degradation of the rubber chewed in shock absorber. 52-372 Table 5: Degradation of the gum without chewing in buffer.

It appears from Tables 4 and 5 that the addition of the enzyme has accelerated the degradation of the chewing gum relative to the chewing gum without enzyme. In addition, the effect of increasing the concentration of the enzyme is an increased degradation. The chewing gum containing glucose oxidase behaved differently from the rest of the samples in that the enzymatic effect revealed different symptoms, that for the chewed gum was a high degree of adhesion, while for the non-chewed gum was the shrinkage . In addition, it should be noted that there are differences in the visible degradation of the chewing gum containing the base for gum 101 and 102, indicating that the results of the enzymatic influence are diverse and depend on the type of polymers used. It is predictable that different gum bases react in different ways with the 52-372 addition of enzymes and it is a matter of designing the appropriate combinations of polymers and enzymes, which provide optimal degradation. This may include both conventional polymers and polymers considered to be biodegradable. In table 6, the results of measuring the pH in the buffer solutions after 10 days are shown: Table 6: pH in the buffer solution after 10 days.

It seems from table 6 that despite the buffer, which was adjusted to pH 5.6, the pH dropped in the solutions surrounding the chewed gum and without chewing, indicating the appearance of degradation. 52-372 Results of the GC / MS evaluation The results of the GC / MS evaluation are presented in figures 1 to 4, which illustrate the formation of two different compounds resulting from the degradation of chewing gum. The figures are related to the following numbers of chewing gum: Figure 1 A and G, Figure 2 A, F and I Figure 3 A, E, H and J Figure 4 A, B, C and D In general, the results confirm Visual observations in which chewing gum containing enzymes are distinguished from chewing gum without enzymes, by the appearance of large amounts of degradation products. Figure 1 shows that one of the degradation products, compound a, has been formed in a larger amount as a result of the addition of an oxidoreductase enzyme, glucose oxidase. Figures 2a and 2b show the increased formation of both degradation products, increasing the amounts of aggregated hydrolase enzyme, neutrase. In Figure 3a it appears that the degradation product, compound a, has been formed in amounts that 52-372 are increased by increasing the bromelain enzyme content in the chewing gum. However, at the larger enzyme content, a smaller amount of the degradation product has been formed. This may be the result of an enzyme overload. It should be expected that the enzyme activity can be prevented at enzyme concentrations beyond a certain optimum concentration, which means that it is a matter of designing the appropriate relationship between the polymer content and the enzyme content in the chewing gum. In Figure 3b it seems that the increase in the concentration of the bromelain enzyme results in a greater formation of the degradation product, compound b, however, the increase in the degradation product between the concentrations of the enzyme of 15% and 45% It is quite low. This again indicates that obtaining an accelerated degradation is a matter of providing an adequate level of concentration of the enzyme. Figures 4a and 4b illustrate the tendency of the increased enzymatic influence on degradation, when the amount of trypsin enzyme concentration is increased in the chewing gum, although the correlation is not categorically proportional. It is generally found that different types of enzyme can show the desired effect of degradation. 52-372 In the present test, both hydrolases and oxidoreductases influenced degradation as catalysts, which can be observed both visually and by GC / MS. It is generally noted that this is not the unambiguous case that the higher concentration of enzyme causes degradation to proceed more rapidly. The relationship between the substrate and the enzyme must be optimized. 2-372

Claims (2)

1. CLAIMS: 1. A chewing gum comprising at least one polymer, chewing gum ingredients and enzymes, wherein at least one of the polymeric forms forms a substrate for at least one of the enzymes. 2. The chewing gum according to claim 1, wherein the chewing gum includes a center filler. 3. The chewing gum according to claim 1 or 2, wherein the chewing gum includes a coating. . The chewing gum according to any of claims 1-3, wherein the ingredients of the chewing gum comprise sweeteners and flavors. 5. The chewing gum according to any of claims 1-4, wherein the ingredients of the chewing gum comprise additional softeners and additives. 6. The chewing gum according to any of claims 1-5, wherein at least one of the polymers forms a base for the chewing gum. 7. Chewing gum according to any of the 52-372 claims 1-6, wherein at least one polymer comprises at least one copolymer. 8. The chewing gum according to any of claims 1-7, wherein at least one copolymer is polymerized from at least two different monomers, each comprising 1-99%. 9. The chewing gum according to any of claims 1-8, wherein at least one polymer comprises at least one biodegradable polymer. 10. The chewing gum according to any of claims 1-9, wherein at least one of the biodegradable polymer comprises at least one biodegradable elastomer. 11. The chewing gum according to any of claims 1-10, wherein at least one of the biodegradable polymer comprises at least one biodegradable elastomeric plasticizer. 12. The chewing gum according to any of claims 1-11, wherein at least one of the biodegradable polymer comprises at least one polyester polymer obtained 52-372 through the polymerization of at least one cyclic ester. 13. The chewing gum according to any of claims 1-12, wherein at least one of the biodegradable polymer comprises at least one polyester polymer obtained by the polymerization of at least one alcohol or a derivative thereof and at least one acid or a derivative thereof. 14. The chewing gum according to any of claims 1-13, wherein at least one of the biodegradable polymer comprises at least one polyester obtained by the polymerization of at least one compound selected from the group of cyclic esters, alcohols or derivatives thereof and carboxylic acids or derivatives thereof. 15. The chewing gum according to any of claims 1-14, wherein the polyester obtained by the polymerization of at least one cyclic ester is at least partially derived from α-hydroxy acids such as lactic and glycolic acids. 16. The chewing gum according to any of claims 1-15, wherein the polyester obtained by the polymerization of at least one cyclic ester is at least 52-372 partially derived from α-hydroxy acids, and wherein the polyester obtained comprises at least 20 mol% of a-hydroxy acid units, preferably at least 50 mol% of α-hydroxy acid units and so still more preferred at least 80% by mol of a-hydroxy acid units. 17. The chewing gum according to any of claims 1-16, wherein at least one or more of the cyclic esters are selected from the groups of glycolides, lactides, lactones, cyclic carbonates or mixtures thereof. 18. The chewing gum according to any of claims 1-17, wherein the lactone monomers are selected from the group of e-caprolactone, d-valerolactone, β-butyrolactone and β-propiolactone, also includes e-caprolactones, d- valerolactones,? -butyrolactones or β-propiolactones which have been substituted with one or more alkyl or aryl substituents on any non-carbonyl carbon atoms along the ring, including the compounds in which two substituents are contained therein carbon atom. 19. The chewing gum according to any of claims 1-18, 52-372 wherein the carbonate monomer is selected from the group of trimethylene carbonate, 5-alkyl-1,3-dioxan-2-one, 5,5-dialkyl-1,3-dioxan-2-one or alkyl-5-alkylcarbonyl-1,3-dioxan-2-one, ethylene carbonate, 3-ethyl-3-hydroxymethyl, propylene carbonate, trimethylpropane monocarbonate, 4,6-dimethyl-l, 3-propylene carbonate, 2, 2-dimethyl trimethylene carbonate and 1,3-dioxepan-2-one and mixtures thereof. 20. The chewing gum according to any of claims 1-19, wherein the cyclic ester polymers and their copolymers resulting from the polymerization of the cyclic ester monomers are comprised of poly (L-lactide); poly (D-lactide); poly (D, L-lactide); poly (mesolactide); poly (glycolide); poly (trimethylene carbonate); poly (epsilon-caprolactone); poly (L-lactide-co-D, L-lactide); poly (L-lactide-co-meso-lactide); poly (L-lactide-co-glycolide); poly (L-lactide-co-trimethylene carbonate); poly (L-lactide-co-epsilon-caprolactone); poly (D, L-lactide-co-meso-lactide); poly (D, L-lactide-co-glycolide); poly (D, L-lactide-co-trimethylene carbonate); poly (D, L-lactide-co-epsilon-caprolactone); poly (meso-lactide-co-glycolide); poly (trimethylene meso-lactide-co-carbonate); poly (meso-lactide-co-epsilon-caprolactone); poly (trimethylene glycolide-co-carbonate); 52-372 poly (glycolide-co-epsilon-caprolactone). 21. The chewing gum according to any of claims 1-20, wherein at least one polymer has a degree of crystallinity in the range of 0 to 95% and more preferably 0 to 70%. 22. The chewing gum according to any of claims 1-21, wherein at least one of the polymer has amorphous regions. 23. The chewing gum according to any of claims 1-22, wherein the polymer is aliphatic. 24. The chewing gum according to any of claims 1-23, wherein the molecular weight of the polymer is within the range of 500-500000 g / mol, preferably within the range of 1500-200000 g / mol of Mn. 25. The chewing gum according to any of claims 1-24, wherein at least one of the enzymes catalyses the degradation of the polymer. 26. The chewing gum according to any of claims 1-25, wherein the chewing gum after being used 52-372 is partially disintegrated due to the influence of enzymes. 27. The chewing gum according to any of claims 1-26, wherein at least one of the enzymes influences the polymeric substrate with a partial disintegration of the chewing gum as a result. 28. The chewing gum according to any of claims 1-27, wherein at least one of the enzymes influences the polymeric substrate with a partial disintegration and a crumbling structure of the chewing gum as a result. 29. The chewing gum according to any of claims 1-28, wherein at least one of the enzymes after using the chewing gum is catalyzed by the degradation of the polymeric substrate until the polymer is completely degraded. 30. The chewing gum according to any of claims 1-29, wherein at least one of the enzymes is active in air and atmospheric pressure and accelerates the degradation of the polymer. 31. The chewing gum according to any of the 52-372 claims 1-30, wherein at least one of the enzymes is contained in the chewing gum, the gum base, the filled center or the coating. 32. The chewing gum according to any of claims 1-31, wherein at least one of the enzymes accelerates the degradation of the polyester obtained by ring opening polymerization of at least one cyclic ester. 33. The chewing gum according to any of claims 1-32, wherein at least one of the enzymes accelerates the degradation of the polyester obtained by the polymerization of at least one alcohol or derivative thereof and at least one acid or derivative thereof. . 34. The chewing gum according to any of claims 1-33, wherein the chewing gum comprises at least one polyester obtained by the ring opening polymerization of at least one cyclic ester and at least one polyester obtained by the polymerization of at least one alcohol or derivative thereof and at least one acid or derivative thereof. 35. The chewing gum according to any of claims 1-34, 52-372 wherein the chewing gum has a water content of less than 10% by weight, preferably less than 5% by weight, more preferably less than 1% by weight and even more preferably less than 0.1% by weight. 36. The chewing gum according to any of claims 1-35, wherein the chewing gum is capable of absorbing water in an amount of at least 0.1% by weight, preferably at least 5% by weight, more preferred at least 10% by weight, even more preferably at least 20% by weight and even more preferably at least 40% by weight. 37. The chewing gum according to any of claims 1-36, wherein the chewing gum comprises a filler in an amount of 0 to 80% by weight. 38. The chewing gum according to any of claims 1-37, wherein the concentration of the enzymes is in the range of 0.0001% by weight to 50% by weight of the chewing gum. 39. The chewing gum according to any of claims 1-38, wherein the concentration of the enzymes is in the range of 0.001% by weight to 10% by weight of the chewing gum. 52-372 40. The chewing gum according to any of claims 1-39, wherein the concentration of the enzymes is in the range of 0.01% by weight to 5% by weight of the chewing gum. 41. The chewing gum according to any of claims 1-40, wherein the amount of the enzymes is in the range of 0.0001 to 80% by weight relative to the amount of the base for the gum in the chewing gum. 42. The chewing gum according to any of claims 1-41, wherein the amount of the enzymes is in the range of 0.001 to 40% by weight relative to the amount of the base for the gum in the chewing gum. 43. The chewing gum according to any of claims 1-42, wherein the amount of the enzymes is in the range of 0.1 to 20% by weight relative to the amount of the base for the gum in the chewing gum. 44. The chewing gum according to any of claims 1-43, wherein at least one of the enzymes is selected from the group consisting of oxidoreductases, transferases, hydrolases, lyases, isomerases and ligases. 52-372 45. The chewing gum according to any of claims 1-44, wherein at least one of the enzymes is an oxidoreductase. 46. The chewing gum according to any of claims 1-45, wherein at least one of the enzymes is a hydrolase. 47. The chewing gum according to any of claims 1-46, wherein at least one of the enzymes is a lyase. 48. The chewing gum according to any of claims 1-47, wherein at least one of the hydrolase enzymes acts on the ester linkages. 49. The chewing gum according to any of claims 1-48, wherein at least one of the hydrolase enzymes is a glycosylase. 50. The chewing gum according to any of claims 1-49, wherein at least one of the hydrolase enzymes acts on the ether linkages. 51. The chewing gum according to any of the 52-372 claims 1-50, wherein at least one of the hydrolase enzymes acts on the carbon-nitrogen bonds. 52. The chewing gum according to any of claims 1-51, wherein at least one of the hydrolase enzymes acts on the peptide bonds. 53. The chewing gum according to any of claims 1-52, wherein at least one of the hydrolase enzymes acts on the acid anhydrides. 54. The chewing gum according to any of claims 1-53, wherein at least one of the hydrolase enzymes acts on the carbon-carbon bonds. 55. The chewing gum according to any of claims 1-54, wherein at least one of the hydrolase enzymes acts on the halide bonds, the phosphorus-nitrogen bonds, the sulfur-nitrogen bonds, the carbon-phosphorus bonds, the bonds Sulfur-sulfur or carbon-sulfur bonds. 56. The chewing gum according to any of claims 1-55, wherein at least one of the enzymes is 52-372 selects from the group of lipases, esterases, depolymerases, peptidases and proteases. 57. The chewing gum according to any of claims 1-56, wherein at least one of the enzymes is an endoenzyme. 58. The chewing gum according to any of claims 1-57, wherein at least one of the enzymes is an exoenzyme. 59. The chewing gum according to any of claims 1-58, wherein at least one of the enzymes has a molecular weight of 2 to 1000 kDa, preferably 10 to 500 kDa. 60. The chewing gum according to any of claims 1-59, wherein at least two of the enzymes are combined. 61. The chewing gum according to any of claims 1-60, wherein at least one of the enzymes requires a cofactor to carry out its catalytic function. 62. The chewing gum according to any of claims 1-61, 52-372 wherein at least one of the enzymes is incorporated in the chewing gum. 63. The chewing gum according to any of claims 1-62, wherein at least one of the enzymes is incorporated in the gum base. 64. The chewing gum according to any of claims 1-63, wherein at least one of the enzymes is incorporated in the coating. 65. The chewing gum according to any of claims 1-64, wherein at least one of the enzymes has an optimum activity in the pH range of 1.0 to 11.0, preferably 4.0 to 8.0 and even more preferred from 4.0 to 6.0. 66. The chewing gum according to any of claims 1-65, wherein at least one of the enzymes has an optimal activity at temperatures in the range of -10 to 60 ° C, preferably from 0 to 50 ° C, more preferably from 5 to 40 ° C and even more preferably from 10 to 40 ° C. 35 ° C. 67. The chewing gum according to any of claims 1-66, 52-372 wherein at least one of the enzymes has an optimum activity under conditions of relative humidity in the range of 10 to 100% RH, preferably 30 to 100% RH. 68. The chewing gum according to any of claims 1-67, wherein the chewing gum is prepared by a one-step process. 69. The chewing gum according to any of claims 1-68, wherein the chewing gum is prepared by a two-step process. 70. The chewing gum according to any of claims 1-69, wherein the chewing gum is prepared by a continuous mixing process. 71. The chewing gum according to any of claims 1-70, wherein the chewing gum is compressed and prepared by the use of compression techniques. 72. The use of at least one enzyme for the degradation of a biodegradable chewing gum. 73. The use of at least one enzyme according to claim 72, wherein at least one enzyme comprises 52-372 hydrolases. 74. A method for the degradation of a biodegradable chewing gum, wherein at least one biodegradable polymer is at least partially degraded by means of at least one enzyme. 75. The method according to claim 74, wherein the enzyme is mixed together with at least one biodegradable polymer by chewing.
2. 2-372