WO2002094959A1 - Procede alcalin ameliore de preparation de colle de poisson de type b - Google Patents

Procede alcalin ameliore de preparation de colle de poisson de type b Download PDF

Info

Publication number
WO2002094959A1
WO2002094959A1 PCT/GB2002/002370 GB0202370W WO02094959A1 WO 2002094959 A1 WO2002094959 A1 WO 2002094959A1 GB 0202370 W GB0202370 W GB 0202370W WO 02094959 A1 WO02094959 A1 WO 02094959A1
Authority
WO
WIPO (PCT)
Prior art keywords
gelatin
process according
skins
fish
range
Prior art date
Application number
PCT/GB2002/002370
Other languages
English (en)
Inventor
David Stanley Field
Original Assignee
Croda International Plc
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 Croda International Plc filed Critical Croda International Plc
Publication of WO2002094959A1 publication Critical patent/WO2002094959A1/fr

Links

Classifications

    • C—CHEMISTRY; METALLURGY
    • C09—DYES; PAINTS; POLISHES; NATURAL RESINS; ADHESIVES; COMPOSITIONS NOT OTHERWISE PROVIDED FOR; APPLICATIONS OF MATERIALS NOT OTHERWISE PROVIDED FOR
    • C09H—PREPARATION OF GLUE OR GELATINE
    • C09H3/00—Isolation of glue or gelatine from raw materials, e.g. by extracting, by heating

Definitions

  • the present invention relates to a method for the manufacture of gelatin from fish collagen, the gelatin thereby produced and its uses, particularly as wall material for hard capsules.
  • the invention relates to an improved alkaline process for producing gelatin having advantageous physical characteristics.
  • gelatin The process of manufacturing gelatin can be traced back over many years. Perhaps the earliest record is that found in the cave paintings of Rekhmara at Thebes, which date back to 1400BC and show the use of animal glue, a low grade of gelatin, in the application of veneers to wooden panels.
  • a useful reference text for the preparation, properties, and applications of gelatin is to be found in the book "The Science and Technology of Gelatin” edited by A.G. Ward and A. Courts, published by Academic Press in 1977.
  • the production of gelatin has grown to be a significant industry and its uses are found to be many and varied. It can be used as a food, although it is deficient in some essential amino acids.
  • Gelatin also has excellent emulsifying and stabilising properties; it is a protective colloid and has useful gel-forming and film- forming properties. Thus, gelatin finds widespread application in many industries, particularly in the food and pharmaceutical industries.
  • Gelatin is a protein derived from the natural protein, collagen, which is found in animal species.
  • the collagen of bone and skin is the primary structural protein in the animal kingdom, and this is the material source used for gelatin manufacture.
  • a major raw material source for gelatin is pigskin.
  • Other major sources are the skins and bones from cattle. Whereas gelatins produced from these raw materials have satisfied the needs of a great many applications over many years, there are certain needs that these raw materials can not satisfy.
  • people who have strict preferences for Kosher or Halal ingredients (such as for foodstuffs) will have had some difficulty, since pigskins and cattle hides and bones are not desirable sources for producing such Kosher and Halal gelatins.
  • Others may have concerns surrounding the onset of Bovine Spongiform Encephalopathy and the perceived risk to health that some associate with products derived from such sources of collagen.
  • An alternative raw material source for producing gelatin is fish collagen, such as is found in fish skins. Careful selection of skins from approved species of fish could therefore allow the production of gelatins that can satisfy Kosher and Halal requirements. Thus, there is an increasing demand for gelatins produced from fish collagen.
  • thermo- reversible gels One of the more important properties of gelatin is its ability to form thermo- reversible gels. This quality can be assessed using a standard test procedure such as the measurement of Bloom Gel Strength (BS 747 1975), and values such as 50-320g can be achieved. Bloom is the force (in grams) required to depress a standard plunger into a set gelatin of 6 2 / 3 % concentration that has been kept at 10°C for 16 hours. This gelling ability is related to both the average molecular weight of the gelatin and to the content of the hydroxyproline and proline amino acids in the collagen used. Whereas the content of these amino acids varies little between species of cattle, pigs and many other warm-blooded animals, there is a significant variation among aquatic species.
  • Table 1 shows the amino acid composition in residues per 1000 residues for bovine gelatin, non-gelling fish gelatin and gelling fish gelatin, respectively:
  • the iso- ionic pH of a gelatin is the pH of a gelatin solution in which there are no other ionic species present (such as when a gelatin solution has been treated with ion-exchange resin).
  • iso-ionic points and iso-electric points are essentially the same.
  • the iso-electric point is the pH at which the gelatin has a net zero charge and thereby shows no net migration on application of an electric field.
  • Fish gelatin and the collagen from which the gelatin is extracted are, as shown in Table 1 , proteins containing about 18 different amino acids.
  • Two of these amino acids, glutamine and asparagine have amide side chains, which can be de-amidated, such as through prolonged exposure to alkaline conditions, to form aspartic and glutamic acids. Exposure to relatively mild acidic conditions does not lead to any significant de-amidation. The de- amidation alters the balance between acidic and basic side chains on the protein, and this accounts for the differences in iso-ionic point of gelatins produced by different processes.
  • Type B gelatins Gelatins produced by an alkaline process (hereinafter referred to as Type B gelatins) generally have an iso-ionic pH (pi) in the range 4.8 - 5.2, whereas gelatins produced by an acidification process (hereinafter referred to as Type A gelatins) generally have an iso- ionic pH in the range of from 6.3 - 9.2.
  • Type B gelatins tend to have higher viscosities than Type A gelatins, and consequently pi can give some indication of the Bloom/viscosity ratio that might be expected.
  • gelatin from fish collagen can prove to be troublesome, and some products may have the undesirable characteristics of fish-like taste or odour.
  • the raw materials also need careful handling and processing to avoid degradation and loss of yield, and to avoid producing a product deemed to be of low quality.
  • British patent specification no. GB 235 635 describes the use of fish offal for the manufacture of gelatin.
  • the disclosed process includes washing, treating with dilute alkali for 18 to 24 hours, washing and, finally, treating with dilute sulphurous acid, a weak acid. Such a process would produce a Type A gelatin.
  • European patent specification no. EP 436 266 discloses a process for preparing fish gelatin comprising (a) treating fish raw material with dilute aqueous alkali, followed by washing with water, (b) treating with dilute aqueous mineral acid, preferably sulphuric acid, followed by washing with water, (c) treating with dilute aqueous organic acid, followed by washing with water and (d) extracting with water at elevated temperatures below 55°C to yield the gelatin product. This process would also produce a Type A gelatin.
  • Type B gelatin would be produced by the process described in US patent specification no. 5 484 888 in which fish skins are soaked in an alkaline solution for 60 days and then the excess alkali is removed before extracting the gelatin from an alkaline solution.
  • the fish gelatin produced using the processes described herein can be used in a wide variety of applications.
  • a particularly useful application is the making of hard capsules, whereby the fish gelatin may be used in forming the walls of the capsules.
  • the use of gelatin in capsule-making has been known for many years since the original disclosures in the early nineteenth century. Current production methods are highly sophisticated operations with high machine outputs and this places key requirements on the quality and consistency of the gelatins used.
  • a typical gelatin specification may include Bloom 235-260 with viscosity 4.3-4.7 mPas (6 2 / 3 % 60°C); for the production of soft capsules, a typical gelatin specification may be Bloom 155-180 with viscosity 3.6-4.2 for a Type B gelatin, or 175-210 Bloom, 2.7-4.2 mPas for a Type A gelatin.
  • Both gelling and non-gelling fish gelatins may be hydrolysed to produce gelatins with relatively low viscosity and low molecular weights. These hydrolysed fish gelatins may be used to advantage in micro-encapsulation, as well as in tabletting and many other applications.
  • the use of hydrolysed gelatin for encapsulation of vitamin E is described in US patent specification no. US 4 395 422.
  • gelatin with excellent properties can be achieved using processing procedures and sequences that are different from those previously disclosed.
  • gelatin of excellent quality can be produced from fish sources according to the method of the present invention. In this process, Type B fish gelatin having a low iso-ionic pH can be obtained.
  • the present invention provides a process for producing, from fish collagen, a type B gelatin having a pi in the range of from 4.5 to 6.0, which process comprises:
  • step (b) acidifying, using a mineral acid, the mixture produced in step (a) to a pH of less than 7;
  • the mixture produced by step (a) has a pH of at least 12, such as about 12.4, and may be as high as 13 or more.
  • a lime slurry in the case where the alkaline medium is lime, a lime slurry may be prepared to a concentration range such as from 0.6 to 8.0% by weight, such as 2-8% by weight, preferably 4-6% and more preferably 1-2%, especially during the early stages of liming, although these quantities could be reduced, if preferred, for the later stages of liming.
  • Step (a) is undertaken to condition the fish skins in the alkaline (eg saturated lime) solution, such that the amide residues are essentially de-amidated.
  • the saturated lime solution and the fish skins are kept in admixture in step (a) for a period in excess of 5 days, and preferably at least 12 days, such as in the range of from 5 to 150 days, such as 15 to 100 days, eg 20 to 70 days.
  • the lime liquors are preferably replaced at intervals throughout the liming process and the fish skins should be agitated and preferably aerated at intervals.
  • the amide residues in the collagen become de-amidated, thereby releasing ammonia; various non- collagenous proteins and other impurities may be solubilised and removed.
  • the lime treatment allows the collagen to become conditioned, such that extraction of gelatin of high quality can be achieved in subsequent processing.
  • the alkaline conditioning of the fish skins in step (a) is not restricted to the use of excess calcium hydroxide (saturated lime slurry) and may be carried out using various other sources of alkaline materials that allow the production of Type B gelatin.
  • Alkaline materials that could be used include, for example, the oxides and hydroxides of alkali or alkaline earth metals, eg sodium, potassium, lithium, calcium, magnesium and the various mixed salts that incorporate such components.
  • solutions of sodium hydroxide of suitable concentration may be used over appropriate time periods.
  • caustic soda is used in step (a) instead of lime
  • 0.6-2% sodium hydroxide solution is preferably used and the mixture with the skins allowed to stand for 1 to 20 days, eg about 4 days.
  • step (a) other additives, such as a swelling suppressant, eg sodium sulphate, may be used, if preferred, to suppress excessive swelling and possible subsequent reduction in gelatin yield.
  • a swelling suppressant eg sodium sulphate
  • step (a) is preceded and/or immediately followed by washing steps.
  • a preparatory alkalination step to pre-condition the skins, without causing substantial de-amidation, may precede liming or other strong alkali treatment.
  • solutions of sodium hydroxide of suitable concentration such as 0.1-1%, eg 0.2%, may be used over appropriate time periods, such as 0 hours to 5 days, eg about 24 hours; other additives, such as a swelling suppressant, eg sodium sulphate, may be used, if desired, as mentioned above, to suppress excessive swelling and possible subsequent loss of gelatin yield.
  • a swelling suppressant eg sodium sulphate
  • frozen or dried skins are used, especially frozen skins, whereby they have been well-preserved.
  • the skins are substantially free of other fish offal, such as bones, flesh, heads, and innards. Still more preferred is when the fish skins are substantially free from the skins or other offal of aquatic mammals, including whales and dolphins.
  • the skins may be in de-scaled form.
  • the fish skins are derived from fish that have evolved in warm water, such as certain tuna species, tilapia and Nile perch. Such warm water species tend to exhibit collagen having the preferred amount of proline and hydroxy-proline residues.
  • the invention further provides a process as described above, wherein the fish skins have a collagen content comprising, per 1000 amino acid residues, more than 110 proline residues and/or more than 60 hydroxyproline residues. In cases where the collagen has an amino acid composition outside these criteria, then steps (a) and (b) are preferably undertaken at a reduced temperature in the range of from about 15 to about 5°C.
  • the acidification step (b) is carried out using a dilute mineral acid, such as dilute sulphuric acid, to enable a pH in the range of from 2 to 6, preferably from 3 to 5, such as 2 to 4, eg about 3.
  • Acidification is most preferably undertaken in the absence of added organic acid(s) and/or in the absence of added sulphurous (SO 2 ) moieties.
  • SO 2 sulphurous
  • the latter results in a product gelatin having a sulphite content of less than 200 ppm and, preferably, less than 50 ppm.
  • the raw material is soaked at the given pH for up to about 24 hours.
  • the acid extraction step (c) is carried out at the lowest temperature possible, typically 30-50°C, although elevation to about 60 to 70°C or higher is practicable, particularly towards the end of the extraction step to help extract all the available gelatin.
  • the acid extraction is preferably carried out at a pH in the range of from 3 to 5, whereby it may not be necessary to add further mineral acid after acidification step (b).
  • step (d) may comprise one or more of the standard separation and/or purification techniques known in the art, including filtration, ion exchange, concentration, sterilisation, drying and the like.
  • step (d) includes an ion-exchange reaction using, for example, both anionic and cationic exchange resin to reduce the salts content of extracted liquors.
  • ion-exchange resins in gelatin manufacture is described by P Caimi in Imaging Science Journal 45 136-138 (1997).
  • Resins can be chosen from any suitable for the purpose, including those manufactured by Rescindion or Rohm & Haas.
  • the fish skins are therefore treated sequentially, preferably in the following stages: defrost the skins, wash, add lime, transfer to process vats (lime pits) and lime for 10 - 100 days, preferably at least 12 days, transfer to washers, wash, add sulphuric acid to pH about 3, transfer to extractors; extract at 40-50°C, filter, de-ionise, evaporate, dry, grind and store.
  • the gelatin thereby produced is of low iso-ionic pH of around 5 because amide-group (- CONH2)-containing amino acids are converted to acid groups (-COOH). More preferably, the raw material and process are chosen so as to result in a gelling gelatin.
  • the present invention further provides a gelatin produced by or producible by the alkaline process according to this invention.
  • a gelatin comprising a thermo-reversible gel at 5% concentration at 20°C.
  • Gelling fish gelatin (Type B) produced by the alkaline process of this invention is particularly suitable for the making of hard and soft capsules. Accordingly, this invention further provides the use of a gelatin, produced by or producible by the alkaline process described herein, in the manufacture of capsules for food and/or pharmaceutical applications, especially a soft capsule comprising such a gelatin.
  • the gelatin of this invention is characterised in having an iso-ionic pH of 4.5 to 6.0, preferably 4.8 to 5.4; the Bloom value is 100 - 320; preferably 230- 270 for hard capsules and 150-200 for soft capsules; the viscosity is 3.0-6.5, preferably 4.0-5.0 mPas (6 2 / 3 %, 60°C) for hard capsules and 3.6-4.2 for soft capsules; and having no or very little odour or taste.
  • These properties may be obtained through blending various extracts of gelatin to give the required characteristics. Thus, individual batches to be included in such blends may cover a wider range of properties such as Bloom 100-320 and viscosity 3.0 - 6.5.
  • the gelatin prepared according to the process of this invention is also suitable for application to the photographic industry, in view of the particularly high purity of the product. Also, this gelatin has a higher methionine content than gelatin of non-fish origin, which provides other advantages in photographic applications. In particular, this gelatin may act as a carrier for the silver nitrate/potassium bromide reaction and protect the resulting crystals as they form. Accordingly, the present invention further provides a photographic composition comprising a gelatin produced by or producible by the alkaline process of this invention.
  • Example 1 Production of Type B Gelatin
  • a sample of frozen tilapia skins was allowed to thaw out in water containing sodium hypochlorite.
  • the skins were given a wash in water (1 hour) to remove some of the fat present.
  • a 2191 g sample of the drained tilapia skins (42 pieces) was placed in a 10-litre container. Water was added to 8 litres and then 100g lime was added.
  • the lime treatment was carried out in the laboratory at ambient temperature (19-25°C). The skins were stirred occasionally. Lime changes were carried out after 5 days and after 34 days by draining off the lime liquor and replacing with water and 100g lime. The skins remained tough throughout the liming period.
  • Extraction A Extraction of Tilapia skins after 42 days in lime
  • the skins were washed in running water over 30 minutes before transferring to a 5 litre polypropylene beaker and covering with water.
  • Sulphuric acid was added over 6 hours to lower the pH to a liquor pH of around pH 3. After 3 hours the liquor pH was 5.0, and the liquor was drained off and replaced with de-ionised water. After a further 2 hours the water was again drained off and replaced with de-ionised water before leaving overnight at pH 3.9. About 18ml concentrated sulphuric acid was used. At this stage, about 20% of the area of the skins was transparent; some skins were swollen and very soft, whereas others were white opaque and quite tough.
  • the gelatin was extracted on heating to 40°C in a water bath over 2-4 hours.
  • the liquor was filtered, de-ionised and the pH adjusted to pH ca 5.5 with sodium hydroxide before allowing to dry on trays at room temperature.
  • Extraction B Extraction of Tilapia skins after 105 days in lime
  • the skins were washed in running water over 30 minutes to remove excess lime. The weight after draining was 2733g.
  • the skins were transferred to a 5 litre polypropylene beaker and covered with water.
  • Sulphuric acid 13ml was added over 3 hours to lower the pH to a liquor pH of around pH 5.5.
  • the liquor was drained off and the skins re-weighed (2075g).
  • De-ionised water was added and a further 5ml sulphuric acid added over 2 hours to give a liquor pH of around 3.0.
  • the skins had swollen and the liquor pH was 4.1.
  • Most of the skins were soft with some transparency, but about 10-20% were white opaque and less soft.
  • the gelatin was extracted on heating to 30-40°C in a water bath over 2-4 hours. The liquor was filtered, de-ionised and allowed to dry on trays at room temperature.
  • Tilapia skins can therefore be used to produce limed gelatin in good yield, and with good chemical and physical properties.
  • Example 2 Starting Material Preparation of Low pi Fish Gelatin using the Liming Process
  • Tilapia skins (2156g) were added to 0.2% sodium hydroxide solution (8064g), mixed and allowed to stand for 24 hours. The sodium hydroxide solution was drained off and the skins rinsed with water (8000g). The skins (3991 g) were then added to a solution of lime (1.2%, 8100g and left for 12 days. After 12 days the lime solution was removed and the skins washed with water (8000g).
  • the skins (3764g) were then added to water (5000g), and the pH adjusted and maintained between 2.5-4.0 with the addition of sulphuric acid (77%) over a period of 6 hours.
  • the skins were then allowed to soak at this pH for a further 17 hours.
  • the acid conditioned skins were then heated to 60°C for 2 hours, whilst maintaining the pH at 4.0 with sulphuric acid (77%). After 2 hours the slurry was coarsely filtered to remove the waste skin residue and the resultant extraction filtrate was filtered through a Dicalite 4258 coated W2 filter pad.
  • Tilapia skins (4341 g) were added to sodium hydroxide solution (1.2%; 19000g), mixed and allowed to stand for 24 hours. The sodium hydroxide solution was then drained off and the skins rinsed with water (19000g). The skins (11297g) were then added to fresh sodium hydroxide (1.2%; 12600g), mixed and allowed to stand for 4 days. The sodium hydroxide solution was then drained off and the skins rinsed with water (12600g).
  • the skins (15224g) were added to water (10000g), and the pH adjusted and maintained between 2.5-4.0 using sulphuric acid (77%) over a period of 6 hours then allowed to soak at this pH for a further 18 hours.
  • the acid conditioned skins were heated to 55°C for 1 1 / 2 hours, whilst maintaining the pH at 4.0 with sodium hydroxide solution (25%). After 1 1 / 2 hours the liquor was coarsely filtered to remove the waste skin residue and the resultant extraction filtrate was filtered through a Dicalite 4258 coated W2 filter pad.
  • the filtrate was then filtered through a BECO-KD5G filter pad to remove the ion-exchange resin, followed by filtration through an XE200H filter pad to clarify.
  • the filtrate was evaporated to 10.2% (9322g) and poured into a tray and allowed to gel at 4°C, noodled, air dried and ground to give low pi Tilapia fish gelatin (906.8g).

Landscapes

  • Chemical & Material Sciences (AREA)
  • Organic Chemistry (AREA)
  • Cosmetics (AREA)
  • Peptides Or Proteins (AREA)
  • Medicinal Preparation (AREA)

Abstract

L'invention concerne un procédé de production de colle de poisson de type B, à partir de collagène de poisson, cette colle présentant un pl compris entre 4,5 et 6. Ce procédé consiste: a) à traiter des peaux de poisson au moyen d'un milieu alcalin pour obtenir un mélange présentant un pH d'au moins 12; b) à acidifier, au moyen d'un acide minéral, le mélange produit lors de l'étape a) jusqu'à obtenir un pH inférieur à 7; et c) à extraire par voie acide la colle produite lors de l'étape c); et facultativement d) à poursuivre le traitement de la colle extraite produite lors de l'étape c). La colle préparée ou pouvant être préparée par le procédé amélioré selon l'invention peut être utilisée dans la fabrication de capsules, en particulier de capsules molles, destinées à des applications alimentaires et/ou pharmaceutiques. Elle peut également être utilisée dans la préparation d'une composition destinée à des applications photographiques.
PCT/GB2002/002370 2001-05-21 2002-05-20 Procede alcalin ameliore de preparation de colle de poisson de type b WO2002094959A1 (fr)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
GB0112331A GB0112331D0 (en) 2001-05-21 2001-05-21 Process
GB0112331.4 2001-05-21

Publications (1)

Publication Number Publication Date
WO2002094959A1 true WO2002094959A1 (fr) 2002-11-28

Family

ID=9915002

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/GB2002/002370 WO2002094959A1 (fr) 2001-05-21 2002-05-20 Procede alcalin ameliore de preparation de colle de poisson de type b

Country Status (2)

Country Link
GB (2) GB0112331D0 (fr)
WO (1) WO2002094959A1 (fr)

Cited By (8)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2003049780A1 (fr) * 2001-12-10 2003-06-19 Tech-Medical S.R.L. Materiau composite biocompatible a action osteotrope
US20110045067A1 (en) * 2008-01-29 2011-02-24 Ayanda As Soft gel capsules
CN102286252A (zh) * 2011-06-21 2011-12-21 郭小棋 一种酸法生产明胶的工艺
CN102702984A (zh) * 2012-06-07 2012-10-03 成都海康生物技术有限公司 一种工业化生产鱼皮明胶的工艺
CN103385864A (zh) * 2012-05-07 2013-11-13 黄族和 一种用鱼皮胶、鱼鳞胶制造药用空心硬胶囊的方法
CN105969203A (zh) * 2016-05-26 2016-09-28 安徽金兑新材料科技有限公司 一种基于动物皮制备皮胶的方法
WO2018066595A1 (fr) * 2016-10-05 2018-04-12 学校法人近畿大学 Composition de collagène
WO2019022623A1 (fr) * 2017-07-26 2019-01-31 Instituto Tecnológico De La Producción Procédé d'obtention de gélatine de peau de poisson au moyen de l'optimisation des conditions d'extraction

Families Citing this family (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2012160575A2 (fr) * 2011-05-18 2012-11-29 GADRE, Arjun Procédé de production de gélatine à partir de poisson
CN107625120A (zh) * 2017-08-01 2018-01-26 霍山县大化坪秀峰茶业精制厂 一种石斛胶囊

Citations (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
FR2365617A1 (fr) * 1976-09-23 1978-04-21 Leiderer Georg Procede pour la preparation de colle et de gelatine
DE2747798A1 (de) * 1977-10-25 1979-04-26 Leon Oudem Verfahren zur extraktion von kollagen und die weiterverarbeitung zu gelatine
US5484888A (en) * 1994-03-08 1996-01-16 Holzer; David Gelatin production
EP1016347A1 (fr) * 1998-12-31 2000-07-05 Skw Biosystems Procédé de préparation de gélatine de poisson

Family Cites Families (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
GB235635A (en) * 1924-03-18 1925-06-18 Joseph Charles Kernot Improvements in and relating to the manufacture of glue, gelatine and meal from fish and other offal of marine origin
IL87344A (en) * 1988-08-04 1992-03-29 Univ Bar Ilan Process for the production of gelatin from fish skins

Patent Citations (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
FR2365617A1 (fr) * 1976-09-23 1978-04-21 Leiderer Georg Procede pour la preparation de colle et de gelatine
DE2747798A1 (de) * 1977-10-25 1979-04-26 Leon Oudem Verfahren zur extraktion von kollagen und die weiterverarbeitung zu gelatine
US5484888A (en) * 1994-03-08 1996-01-16 Holzer; David Gelatin production
EP1016347A1 (fr) * 1998-12-31 2000-07-05 Skw Biosystems Procédé de préparation de gélatine de poisson

Cited By (9)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2003049780A1 (fr) * 2001-12-10 2003-06-19 Tech-Medical S.R.L. Materiau composite biocompatible a action osteotrope
US20110045067A1 (en) * 2008-01-29 2011-02-24 Ayanda As Soft gel capsules
CN102286252A (zh) * 2011-06-21 2011-12-21 郭小棋 一种酸法生产明胶的工艺
CN103385864A (zh) * 2012-05-07 2013-11-13 黄族和 一种用鱼皮胶、鱼鳞胶制造药用空心硬胶囊的方法
CN102702984A (zh) * 2012-06-07 2012-10-03 成都海康生物技术有限公司 一种工业化生产鱼皮明胶的工艺
CN102702984B (zh) * 2012-06-07 2014-05-07 成都海康生物技术有限公司 一种工业化生产鱼皮明胶的工艺
CN105969203A (zh) * 2016-05-26 2016-09-28 安徽金兑新材料科技有限公司 一种基于动物皮制备皮胶的方法
WO2018066595A1 (fr) * 2016-10-05 2018-04-12 学校法人近畿大学 Composition de collagène
WO2019022623A1 (fr) * 2017-07-26 2019-01-31 Instituto Tecnológico De La Producción Procédé d'obtention de gélatine de peau de poisson au moyen de l'optimisation des conditions d'extraction

Also Published As

Publication number Publication date
GB0211556D0 (en) 2002-06-26
GB0112331D0 (en) 2001-07-11
GB2377708B (en) 2003-08-27
GB2377708A (en) 2003-01-22

Similar Documents

Publication Publication Date Title
US5093474A (en) Process for the production of gelatin from fish skins
US6368656B1 (en) process for the preparation of fish gelatin
RU2126434C1 (ru) Способ получения желатина из коллагенсодержащего сырья
US5484888A (en) Gelatin production
US3073702A (en) Water dispersible collagen
WO2002094959A1 (fr) Procede alcalin ameliore de preparation de colle de poisson de type b
JP4226299B2 (ja) 魚由来ゼラチンペプチドの製造方法
KR100679712B1 (ko) 불가사리로부터 콜라겐을 제조하는 방법
KR102448117B1 (ko) 어포 제조방법 및 그 어포
US4309794A (en) Method for the separation of fat, pigments and entrail remains from fish raw material
KR100532153B1 (ko) 어류 비늘을 이용한 단백질 가수분해물의 제조방법
US5908921A (en) Method of manufacturing gelatin
EP1367066A2 (fr) Gélatine succinylée de poisson
Shakil et al. Tannery solid waste into wealth by non-edible gelatin production from raw trimmings
WO2002094958A1 (fr) Procede acide ameliore pour la preparation de gelatine de poisson de type a
AU6914701A (en) Method for the production of gelatin of marine origin and product thus obtained
KR20190065935A (ko) 마린 콜라겐의 대량생산을 위한 고순도 정제방법
JP2010241708A (ja) エラスチン含有可溶性ペプチド及びその製造方法
RU2722210C1 (ru) Способ получения рыбного желатина
KR100487994B1 (ko) 어류 젤라틴의 제조방법
JPH05155900A (ja) 高純度の酸不溶性魚鱗コラーゲンおよびその製造法
Lüpke et al. Gas chromatographic evaluation of amino acid epimerisation in the course of gelatin manufacturing and processing
SU971223A1 (ru) Способ получени корма из отходов кожевенного производства
SU1084004A1 (ru) Способ производства кормовой добавки из дубленых отходов кожевенного производства
SU1028236A3 (ru) Способ получени кормовых средств из протеинсодержащих отходов переработки животного сырь

Legal Events

Date Code Title Description
AK Designated states

Kind code of ref document: A1

Designated state(s): AE AG AL AM AT AU AZ BA BB BG BR BY BZ CA CH CN CO CR CU CZ DE DK DM DZ EC EE ES FI GB GD GE GH GM HR HU ID IL IN IS JP KE KG KP KR KZ LC LK LR LS LT LU LV MA MD MG MK MN MW MX MZ NO NZ OM PH PL PT RO RU SD SE SG SI SK SL TJ TM TN TR TT TZ UA UG US UZ VN YU ZA ZM ZW

AL Designated countries for regional patents

Kind code of ref document: A1

Designated state(s): GH GM KE LS MW MZ SD SL SZ TZ UG ZM ZW AM AZ BY KG KZ MD RU TJ TM AT BE CH CY DE DK ES FI FR GB GR IE IT LU MC NL PT SE TR BF BJ CF CG CI CM GA GN GQ GW ML MR NE SN TD TG

DFPE Request for preliminary examination filed prior to expiration of 19th month from priority date (pct application filed before 20040101)
121 Ep: the epo has been informed by wipo that ep was designated in this application
REG Reference to national code

Ref country code: DE

Ref legal event code: 8642

122 Ep: pct application non-entry in european phase
NENP Non-entry into the national phase

Ref country code: JP

WWW Wipo information: withdrawn in national office

Country of ref document: JP