EP3439490A1 - Fraction protéique végétale techno-fonctionnelle obtenue à partir de légumineuses ou de graines oléagineuses - Google Patents

Fraction protéique végétale techno-fonctionnelle obtenue à partir de légumineuses ou de graines oléagineuses

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Publication number
EP3439490A1
EP3439490A1 EP17719814.0A EP17719814A EP3439490A1 EP 3439490 A1 EP3439490 A1 EP 3439490A1 EP 17719814 A EP17719814 A EP 17719814A EP 3439490 A1 EP3439490 A1 EP 3439490A1
Authority
EP
European Patent Office
Prior art keywords
protein fraction
protein
fraction
water
vegetable
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Withdrawn
Application number
EP17719814.0A
Other languages
German (de)
English (en)
Inventor
Isabel MURANYI
Claudia Pickardt
Daniela SUSSMANN
Pia MEINLSCHMIDT
Peter Eisner
Ute SCHWEIGGERT-WEISZ
Arne KEITZEL
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Fraunhofer Gesellschaft zur Forderung der Angewandten Forschung eV
Original Assignee
Fraunhofer Gesellschaft zur Forderung der Angewandten Forschung eV
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Fraunhofer Gesellschaft zur Forderung der Angewandten Forschung eV filed Critical Fraunhofer Gesellschaft zur Forderung der Angewandten Forschung eV
Publication of EP3439490A1 publication Critical patent/EP3439490A1/fr
Withdrawn legal-status Critical Current

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Classifications

    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
    • A23J1/14—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from leguminous or other vegetable seeds; from press-cake or oil-bearing seeds
    • A23J1/148—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from leguminous or other vegetable seeds; from press-cake or oil-bearing seeds by treatment involving enzymes or microorganisms
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J3/00—Working-up of proteins for foodstuffs
    • A23J3/14—Vegetable proteins
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J3/00—Working-up of proteins for foodstuffs
    • A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
    • A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
    • A23J3/34—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes
    • A23J3/346—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of vegetable proteins
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
    • A23L11/00—Pulses, i.e. fruits of leguminous plants, for production of food; Products from legumes; Preparation or treatment thereof
    • A23L11/30—Removing undesirable substances, e.g. bitter substances
    • A23L11/31—Removing undesirable substances, e.g. bitter substances by heating without chemical treatment, e.g. steam treatment, cooking
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
    • A23L11/00—Pulses, i.e. fruits of leguminous plants, for production of food; Products from legumes; Preparation or treatment thereof
    • A23L11/30—Removing undesirable substances, e.g. bitter substances
    • A23L11/33—Removing undesirable substances, e.g. bitter substances using enzymes; Enzymatic transformation of pulses or legumes
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
    • A23L11/00—Pulses, i.e. fruits of leguminous plants, for production of food; Products from legumes; Preparation or treatment thereof
    • A23L11/30—Removing undesirable substances, e.g. bitter substances
    • A23L11/37—Removing undesirable substances, e.g. bitter substances using microorganisms
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
    • A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
    • A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
    • A23L33/17—Amino acids, peptides or proteins
    • A23L33/185—Vegetable proteins
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
    • A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs

Definitions

  • the invention relates to a vegetable protein fraction from legumes or oilseeds containing one or more
  • Vegetable proteins are becoming increasingly popular among consumers. Today, a variety of different plant proteins from legumes, oilseeds or cereals are already being used in foods as texturizing agents
  • Components used They are used to stabilize emulsions, foams or the formation of gels or are added to foods or beverages for enrichment with proteins as the most readily soluble component.
  • Hydrolysis of plant proteins is a known method of altering the properties of proteins such as techno-functionality (e.g., protein solubility,
  • Emulgier Dam, foaming or the allergenicity of the preparations. Described are protein hydrolysates based on vegetable proteins and based on whey proteins.
  • Protein fractions primarily the permeate, obtained in a downstream process by ultrafiltration and / or soluble and insoluble proteins by a separation.
  • further processing steps follow, such as a subsequent drying process (e.g., freeze-drying) of the products.
  • Hydrolysis is carried out under optimal pH and temperature conditions with the help of at least two proteases to a degree of hydrolysis of 15-35% without pH regulation and the enzymes after a hydrolysis of> 14 hours by a
  • Heat treatment inactivated are used.
  • further processing steps such as spray drying for concentration and drying of the products follow. However it does not address the techno-functional properties and immunoreactivity. Due to the high
  • the degree of hydrolysis, the long treatment time when using Alcalase and the subsequent ultrafiltration can be assumed that the techno-functional properties such as the emulsifying capacity, the foam stability and the
  • the whey protein is previously recovered by an acid precipitation from casein.
  • a cut-off of> 10,000 Da, preferably> 50,000 Da is set in the separation by means of ultrafiltration by selecting the membranes.
  • EP0421309 describes a process for producing a whey protein hydrolyzate and combinations thereof with soy protein or casein. Prior to enzymatic hydrolysis, large proteins (> 50,000 Da) are separated by ultrafiltration. Subsequent to the enzymatic hydrolysis with the aid of an enzyme combination is a
  • EP1236405 describes a process for producing hypo-allergenic, soy-based products whose antigenicity is reduced by a factor of 100 (inhibition ELISA). In this case, a moderate degree of hydrolysis of ⁇ 25%, preferably between 10-20%, is desired. It is possible to use either single enzymes of a microbial or plant origin or one Combination of these can be used. The enzyme to substrate ratio ⁇ (E / S) is between 0.1-10%, and the hydrolysis takes place between 0.5-10 hours. When an enzyme combination is used as a two-step process, there must always be one between enzyme addition
  • the resulting hydrolyzate can optionally be separated by ultrafiltration or separation of insoluble proteins.
  • the techno-functional and sensory properties of the products are not reported. However, it can be expected that the use of higher E / S ratios and the use of Alcalase will again result in degraded techno-functionality of the products. In addition, it is known that Alcalase treatment leads to high bitterness, which in turn is consumer acceptance
  • EP1512328 For the hydrolysis of a "soy paste" with 10-20% soy protein, a fungal protease or a combination is used as a one-step process of fungal proteases possessing both endo and exoproteolytic activities, where Corolase PN-L (Aspergillus sojae) and Flavourzyme 500L (Aspergillus oryzae) listed. After a treatment time of 0.5-5 hours, the enzymes are inactivated by a thermal step and the soluble and insoluble protein fraction separated by centrifugation and then dried. About Immunreak ⁇ tivity or Allergenicity is not reported, and only the soluble protein fraction with its high functionality is emphasized, the insoluble (modified) proteins or the mixed protein fraction are not further described.
  • EP0406598A1 describes a method of reducing the Bitterness of enzymatically hydrolysed proteins.
  • protein hydrolysates are subjected to a subsequent fermentation for up to 30 hours at a constant pH value in order to attenuate the bitterness.
  • the literature also describes that the fermentation has a negative influence on the emulsifying properties of legume proteins.
  • the example of lupine proteins was described in P. Eisner, "Extractive fractionation of Legume seed "habilitation 2014, Technical University of Kunststoff, shown that the emulsifying ⁇ capacity g drops / at Lupinenproteinisolaten of 510 mL to values of 385-230 mg / L, for the recovery of functional food ingredients the example of the Lupine when the protein with Lb. perolens, Pc pentosaceus, Lb. plantarum or Lc. paracasei.
  • the emulsification capacity of 660 mL / g dropped to values between 475-483 mL / g
  • the protein solubility at pH 7 dropped from 44.0% to values between 16.5- 18.2% when the protein was incubated with Lb. helveticus was fermented for 24 and 48 hours.
  • a person skilled in the art who would like to provide a highly functional protein preparation with good emulsifying properties would therefore try to avoid fermentation as a processing step.
  • enzyme combinations are very often used for the treatment of proteins.
  • hydrolysates e.g. obtained by ultrafiltration a low molecular weight fraction whose immunoreactivity is described as reduced.
  • the separated small molecule fragments hardly emulsify, form stable foams and often have a very bitter and almost repulsive taste.
  • the object of the present invention is a plant protein fraction and a method for producing the vegetable protein fraction from proteins of legumes (eg soybean, pea, lupine, bean, chickpea, lentil or peanut) or oilseeds (eg sunflower, rape, Camelina or flax) which has a reduced immunoreactivity
  • legumes eg soybean, pea, lupine, bean, chickpea, lentil or peanut
  • oilseeds eg sunflower, rape, Camelina or flax
  • the protein fractions produced should in particular have a light color and good emulsifying properties, taste almost neutral, and in particular have a low bitterness and barely perceptible beany taste.
  • the method used for this should be cost-effective and show a high yield, since in the prior art often only small fractions of the proteins from the raw materials are recyclable, resulting in very high costs.
  • a protein fraction from legumes or oilseeds is understood below to mean a mixture of different proteins from seeds of legumes or oilseeds which do not differ from the protein composition (quantitative ratio). proteins) from the corresponding plant seeds
  • peptide strands may contain separated peptide strands.
  • Protein fraction of comminuted plant seeds in a fractionation step hereinafter also referred to as first fractionation step
  • thermally hydrolyzed protein fraction preferably after the addition of microorganisms (at least 10 8 CFU per gram of protein, more preferably> 10 9 cfu per gram of protein, advantageously ⁇ 10 10 cfu per gram of protein; CFU: colony ⁇ forming unit) and in the presence of glucose or a other easy to ferment carbohydrate, f) pressure and / or shear treatment of the hydrous
  • step e by centrifugation or membrane filtration with a suitable cut-off after (optional) fermentation (step e)) or without fermentation after hydrolysis (step c))
  • the separation by size can be carried out, for example, by various filtration methods, e.g. Membrane filtration (e.g., filtration, microfiltration, ultrafiltration), sedimentation separation by methods utilizing inertia, e.g.
  • a solvent-based separation can take place.
  • the seeds or a mechanically pretreated fraction of the seeds (referred to below as the raw material) are brought into contact with polar or nonpolar solvents, whereby one protein fraction enters the solvent and another protein fraction remains in the raw material.
  • solvent can be used, for example, water, acidified water, critical C02, ethanol, water-ethanol mixtures and hexane. At least one of the protein fractions (first or second protein fraction) is then subjected to the process described under b) -h).
  • the water-containing ⁇ (plant) according to the invention obtained by the process according to protein fraction can carry out the process steps mentioned in the moist state directly in
  • the process steps of hydrolysis, fermentation, pressure ⁇ treatment, heating, pressure and / or shear stress and filtration / centrifugation can be used according to the invention more than once in different orders to further improve the sensory and functional properties.
  • the fermentation follows the
  • Enzyme treatment and the pressure and / or shear treatment of the fermentation wherein the heating steps are at any positions in this order, i. also between fermentation and enzyme treatment and / or between pressure and / or
  • the pressure and / or shear treatment specified under f) is carried out in the process according to the invention at a pressure above 2 * 10 5 Pa (2 bar), advantageously above 5 * 10 5 Pa (5 bar), particularly advantageously at a pressure above of 150 * 10 5 Pa (150 bar). It shows up in Try increasing the pressure to a maximum pressure of 1000 * 10 5 Pa (1000 bar) to obtain the
  • Protein functionality should not be exceeded, and simultaneous shearing (for example with the aid of a homogenizer) the solubility and usually also the emulsifying properties of the water-containing protein fraction can be improved.
  • step h In order to verify the effectiveness of the filtration / centrifugation in step h), in the case of one in the process
  • Microorganisms are used. If successful
  • Separation method are preferably found in the residue more than 50% by mass of the originally introduced for the fermentation microorganisms DNA and in the supernatant less than 20 mass%.
  • crushed legume seeds or oilseeds used in the method according to the invention are crushed legume seeds or oilseeds used in the method according to the invention.
  • Particles or pieces of seeds which are modified by a mechanical process e.g., mill, roller mill, or the like
  • a mechanical process e.g., mill, roller mill, or the like
  • microorganisms come from the groups lactic acid bacteria (Lb. perolens), yeasts (e.g.
  • Saccharomyces cerevisiae Saccharomyces cerevisiae
  • fungal cultures e.g., Rhizopus oryzae, Actinomucor elegans.
  • Protein fraction also change the immunoreactivity in the course of fermentation another, although the same
  • Microorganisms are used. Therefore, it should be ensured that after adding the water until the
  • the mass ratio of water to protein as possible higher than 1: 1, better higher than 8: 1, particularly advantageously higher than 16: 1.
  • a drying step should take place only after the pressure / shear treatment according to the invention.
  • the treated by enzymatic and / or fermentative methods proteins from the mentioned raw materials should be readily dispersible in water or at least in water, so that the enzymatic treatment can be controlled through ⁇ .
  • the process is carried out particularly advantageously if at least 35% of the protein constituents are dissolved at pH 7 or are present in a stable dispersion.
  • the raw materials are mixed with water, dissolved or dispersed and added the enzymes in appropriate concentrations.
  • Stable dispersion means the proportion of dispersed particles of a dispersion which, after a sedimentation time of 10 minutes, are still in the supernatant above a separated sediment.
  • the solvent for separating the first protein fraction may consist of or consist of water or aqueous solutions
  • Soy protein after extraction and isoelectric precipitation at a value of about 2 is to be reduced to values below 1, and simultaneously to generate attractive flavor notes in the protein ⁇ fraction.
  • treated fermentation is preferably carried out with lactic acid bacteria ⁇ , then the protein fraction at a pressure of about 2 ⁇ 10 5 Pa (2 bar) and then
  • Microbial load in the protein fraction also other sensory effects can be achieved by thermally induced reactions, which have a positive effect on consumer acceptance.
  • ⁇ protein fraction is heated more than 1 time to values above 80 ° C during treatment advantageous, particularly advantageously more than 3 times.
  • Emulsifying capacity results when, after hydrolysis and (optional) fermentation, a separation step is carried out by size or solubility or sedimentation, e.g. a centrifugation or filtration. It shows that the protein fraction in the sediment in comparison to the protein fraction in the supernatant after centrifugation despite similar
  • Permeate protein fractions after ultrafiltration Again, the retentate fraction is better suited as an emulsifier, but produces stronger allergic reactions in prick tests in human skin.
  • Processes according to the invention obtained protein fractions are the retentate fraction or sediment fraction and the permeate fraction or supernatant fraction.
  • the protein fraction according to the invention contains more than
  • the protein fraction according to the invention may consist of one or a mixture of several partial fractions of the respective entirety of
  • Proteins consist of the raw materials mentioned.
  • the protein fraction after fermentation has a proportion of biomass from microorganisms which
  • Dry matter content based on the dry matter content of the protein fraction greater than 0.05 mass%, better greater than 0.5 mass%, particularly advantageously greater than 1 mass%. It turns out that an enrichment of biomass
  • Lactic acid bacteria up to a proportion of 1 mass%
  • Microorganism dry matter the protein fraction as Sensory is increasingly appealing. At higher concentrations the popularity decreases again.
  • the protein fraction according to the invention preferably consists of a proportion of protein which is soluble at pH 7 and of a proportion of protein which is insoluble at pH 7.
  • the soluble fraction of the protein fraction surprisingly has a narrow molecular weight distribution.
  • the molecular sizes are more than 30% less than 25 kDa, preferably more than 50%, particularly preferably more than 90%. Therefore, the properties of the proteins of the soluble portion are very uniform. It would thus be possible to separate the soluble fraction at pH 7 from the insoluble one and use both protein fractions separately.
  • the soluble fraction there are a variety of
  • Production is the protein fraction according to the invention only by the permeate or supernatant fraction or through the
  • Retentate or sediment fraction is formed and then has a molecular weight distribution, wherein the molecule sizes are either more than 50% less than 25 kDa, preferably more than 70%, more preferably more than 90%, or less than 60% the molecular sizes are less than 25 kDa, preferably less than 50%, more preferably less than 20%.
  • the protein fraction according to the invention advantageously has a foam activity (based on a starting solution) of greater than 1000%, preferably greater than 1500%, particularly preferably greater than 2000%.
  • the emulsifying capacity is preferably> 200 ml oil / g protein, particularly advantageously> 500 ml oil / g protein and preferably - after sufficient pressure and shear treatment - a solubility of> 25% at pH 7.
  • this value is above 70, preferably above 80, particularly advantageously above 90.
  • the color of the protein fraction thus falls according to the invention very bright and ranges depending on predominantly contained
  • the protein fraction advantageously contains a proportion of aroma components derived from the fermentation, such as diacetyl or other metabolites of the fermentative
  • the immunoreactivity of the product according to the invention is reduced by at least 50%, better by> 80%, compared to a native protein from the same plant. This value is determined by the evaluation of a Western Blot.
  • Protein fractions from plant proteins with the following
  • Protein solubility at pH 4 Protein solubility at pH 4
  • Standardized Food Protein Solubility Procedure Journal of Food Science 50: 1715-1718 is greater than 5%, preferably greater than 20%
  • the protein solubility determined according to Morr et al. 1985 is preferably greater than 25%, preferably greater than 50%. Typically, the protein solubility is in the range of> 35-90%.
  • the emulsifying capacity determined by the conductance measurement method, amounts to at least 200 ml oil / g, preferably at least 500 ml oil / g.
  • the water binding determined by the AACC determination method, is at least 2 ml / g, preferably at least 3 ml / g.
  • the oil binding determined by the fat binding method, is at least 1 ml / g, preferably at least 2 ml / g.
  • the foam activity is at least 1000%.
  • Foam density is in the range of 30 to 220 g / 1.
  • the foam stability is at least 2%, preferably at least 50%.
  • the protein fraction is in the
  • Protein fraction are such that, when incorporated into food and feed, essentially no significant change of the species-specific, as determined by conventional statistical methods, is made
  • Protein fraction are such that, when incorporated into food and feed, essentially no significant change of the species-specific, as determined by conventional statistical methods, is made
  • Aroma change which is caused in a food preparation by the use of the protein fraction, compared to the food preparation without the protein fraction is limited to such an extent that a trained examiner a deviation of any of the above taste or aroma features on a
  • the protein fraction according to the invention may therefore have one or more of the above techno-functional and sensory properties.
  • the protein fraction according to the invention is preferably used as a food ingredient. Since, in addition to the improved functionality and sensor technology, the immunoreactivity of the protein fraction according to the invention is markedly reduced, the protein fraction from a raw material (for example soya or sunflower) or mixtures of different raw materials may advantageously be hypoallergenic or allergen-reduced
  • Protein ingredient used in food Protein ingredient used in food.
  • Textile effects e.g., stabilization of emulsions
  • Textile effects can be further reduced, as compared to previously available protein ingredients on the market
  • extruded wet or dry protein products such as herbal meat alternatives from cooking extrusion or herbal dry extrudates.
  • a soy protein fraction was obtained which was extracted by aqueous extraction at pH 8 from ground and water-extracted soybeans and concentrated with a precipitate at the isoelectric point. The resulting suspension was neutralized and taken to a Protein: water ratio adjusted to 1:20. Afterwards, the following process steps were carried out:
  • the protein fraction obtained has an almost white
  • Protein fraction is used for the following determination methods:
  • the protein content is defined as the content calculated from the determination of nitrogen (N) and its multiplication by a factor of 6.25.
  • the protein content is z. B. in percent based on the dry mass (TS) indicated.
  • - Color The perceptible color is defined by CIE-L * a * b * -
  • the L * axis indicates the brightness, where black is 0 and white has the value 100, the a * -axis describes the green or red part and the b * -axis the blue part or yellow part.
  • Protein solubility (at pH 7 or pH 4):
  • Protein solubility is determined by Morr's assay method (Morr et al., "A Collaborative Study on Developing a Standardized Food Protein Solubility Procedure", Journal of Food Science 50: 1715-1718).
  • the protein fraction is suspended to a mass volume fraction of 1:25 to 1:50 (w / v) (ie 1-2 g of the protein fraction to 50 ml of solution) in a 0.1 M NaCl solution at room temperature and using held for about 60 min at a pH of pH 7 (or pH 4) and stirred at about 200 U / mm and the insoluble sediment then centrifuged for 15 min at 20,000 xg of 0.1 M HCl or NaOH solution ,
  • the protein solubility is e.g. in percent, where a protein solubility ⁇ X "6 means that x% of the protein present in the protein fraction is recovered in the clarified supernatant when the said method is used.
  • the water binding capacity is defined by means of determination methods (here called AACC determination method) as indicated in: American Association of Cereal Chemists, "Approved Methods of the AACC". 10th ed., AACC. St. Paul, MN, 2000; Method 56-20. "Hydration capacity of pregelatinized cereal products”.
  • the water binding capacity is z. In ml / g, i. E. Milliliters of bound water per gram
  • Protein fraction is determined by the weight of the water-saturated according to the AACC determination method
  • the oil-binding capacity is determined by means of determination methods (here Fat binding method), as indicated in: Ludwig I. et al. , "A Micrometer for Determining Fat Binding Capacity". Food / Food, 33 (1), 99.
  • the oil-binding capacity is given in ml / g, ie
  • Milliliters of bound oil per gram of protein fraction is prepared according to o. Determination method measured as volume of oil-binding sediment after mixing 1.5 g protein fraction with 15 ml corn oil for 1 minute and centrifuging at 700 g for 15 minutes at 200 ° C.
  • the emulsifying capacity is determined by means of determination method (here called conductivity measurement method) in which a 1% suspension of the protein fraction of 100 ml, pH 7, corn oil is added until the phase inversion of the oil-in-water emulsion.
  • the emulsifying capacity is defined as the maximum oil absorption capacity of this suspension, determined by the spontaneous decrease in the conductivity of the suspension
  • Phase inversion (A.A., A., et al., "New Processing of Lupine Protein Isolates and Functional Properties.” Food / Food 45: 393-395) and is used e.g. expressed in ml of oil / g, d. H.
  • the foam activity is given in percent, measured as the volume increase of a 5% protein solution, pH 7
  • Hobart 50N standard food processor (5 liter steel kettle) with whisk (wire brush).
  • the foam density is given in g / 1, d. H. Mass of the
  • Foam per unit volume is measured after adding a 5% protein solution, pH 7, from 8 min to level 3 (591 rpm) in a Hobart 50N standard food processor
  • the foam stability is given in percent, measured as the remaining volume of 100 ml of foam within one hour after loading a 5% protein solution, pH 7, 8 min at level 3 (591 rpm) in a Hobart 50N standard food processor (steel kettle with 5 liters content) with whisk (wire brush).
  • Yellowness concentration is defined by determination method as indicated in: Sathe SK et al. .
  • the molecular weight distribution is by means of
  • the degree of hydrolysis is defined by means of determination methods (here called DH value analysis), as indicated in: Nielsen P.M. et al. , "Improved method for determining the protein-protein degree of hydrolysis.” Journal of Food Science
  • the immunoreactivity is by means of determination methods (Sandwich ELISA and Western Blot) as defined: Meinlschmidt P. et al. , "Immunoreactivity, sensory and physicochemical properties of fermented soy protein isolates", Food Chemistry 205: 229-238.
  • the quantification of the microorganisms can be carried out by microscopic methods or by quantification of the DNA strands contained in the protein fraction
  • the quantification of the DNA strands is carried out with a molecular biological method, which under the
  • Examples of taste or aroma impressions to be tested are:
  • Peppers or green peas are Peppers or green peas
  • the panel was previously using a sensory input

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  • Engineering & Computer Science (AREA)
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  • Polymers & Plastics (AREA)
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  • Agronomy & Crop Science (AREA)
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  • Chemical Kinetics & Catalysis (AREA)
  • General Chemical & Material Sciences (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Mycology (AREA)
  • Peptides Or Proteins (AREA)
  • Coloring Foods And Improving Nutritive Qualities (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)

Abstract

L'invention concerne une fraction protéique végétale obtenue à partir de légumineuses ou de graines oléagineuses, destinée à être utilisée dans des denrées alimentaires ou des aliments pour animaux, ainsi qu'un procédé permettant de fabriquer ladite fraction protéique végétale. Dans le procédé, une première fraction protéique est séparée des légumineuses ou graines oléagineuses broyées, à l'aide d'un solvant, ce qui produit seconde fraction protéique résiduelle, puis une fraction protéique aqueuse obtenue par cette étape de fractionnement de façon directe ou après l'ajout d'eau est soumise à un traitement unique ou répété au moyen d'enzymes, à un chauffage unique ou répété à une température > 70 °C, éventuellement à une fermentation unique ou répétée et à un traitement par pression et/ou cisaillement unique ou répété. La fraction protéique végétale fabriquée par ce procédé présente une immunoréactivité réduite et dispose de bonnes caractéristiques techno-fonctionnelles et organoleptiques.
EP17719814.0A 2016-04-08 2017-04-06 Fraction protéique végétale techno-fonctionnelle obtenue à partir de légumineuses ou de graines oléagineuses Withdrawn EP3439490A1 (fr)

Applications Claiming Priority (2)

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DE102016106465 2016-04-08
PCT/EP2017/058187 WO2017174699A1 (fr) 2016-04-08 2017-04-06 Fraction protéique végétale techno-fonctionnelle obtenue à partir de légumineuses ou de graines oléagineuses

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EP3439490A1 true EP3439490A1 (fr) 2019-02-13

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US (1) US20190124946A1 (fr)
EP (1) EP3439490A1 (fr)
JP (1) JP2019513380A (fr)
KR (1) KR20180130530A (fr)
CN (1) CN109310128A (fr)
BR (1) BR112018070543A2 (fr)
WO (1) WO2017174699A1 (fr)

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FR3090279B1 (fr) * 2018-12-21 2020-12-25 Roquette Freres Produit sec base pois pour alimentation des animaux
FI128824B (en) * 2019-07-25 2020-12-31 Avena Nordic Grain Oy A process for preparing a vegetable protein ingredient
IL288258B2 (en) * 2021-11-21 2023-08-01 More Alternative Foods Ltd Meat substitute products that include oilseed solids
CN116656763B (zh) * 2023-07-25 2023-10-13 山东山歌食品科技股份有限公司 一种花生抗氧化肽的制备方法

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US20190124946A1 (en) 2019-05-02
CN109310128A (zh) 2019-02-05
WO2017174699A1 (fr) 2017-10-12
KR20180130530A (ko) 2018-12-07
JP2019513380A (ja) 2019-05-30
BR112018070543A2 (pt) 2019-02-12

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