WO2002089607A1 - Procédé pour lier de la viande et du poisson - Google Patents

Procédé pour lier de la viande et du poisson Download PDF

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Publication number
WO2002089607A1
WO2002089607A1 PCT/NL2002/000293 NL0200293W WO02089607A1 WO 2002089607 A1 WO2002089607 A1 WO 2002089607A1 NL 0200293 W NL0200293 W NL 0200293W WO 02089607 A1 WO02089607 A1 WO 02089607A1
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WO
WIPO (PCT)
Prior art keywords
solution
fibrinogen
reducing agent
transglutaminase
meat
Prior art date
Application number
PCT/NL2002/000293
Other languages
English (en)
Inventor
Govardus Adrianus Hubertus De Jong
Gerrit Wijngaards
Original Assignee
Nederlandse Organisatie Voor Toegepastnatuurwetenschappelijk Onderzoek Tno
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 Nederlandse Organisatie Voor Toegepastnatuurwetenschappelijk Onderzoek Tno filed Critical Nederlandse Organisatie Voor Toegepastnatuurwetenschappelijk Onderzoek Tno
Publication of WO2002089607A1 publication Critical patent/WO2002089607A1/fr

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Classifications

    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y203/00—Acyltransferases (2.3)
    • C12Y203/02—Aminoacyltransferases (2.3.2)
    • C12Y203/02013—Protein-glutamine gamma-glutamyltransferase (2.3.2.13), i.e. transglutaminase or factor XIII
    • 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
    • A23J3/04—Animal proteins
    • A23J3/06—Gelatine
    • 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
    • A23J3/04—Animal proteins
    • A23J3/08—Dairy proteins
    • A23J3/10—Casein
    • 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
    • A23J3/04—Animal proteins
    • A23J3/12—Animal proteins from blood
    • 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
    • A23L13/00—Meat products; Meat meal; Preparation or treatment thereof
    • A23L13/03—Coating with a layer; Stuffing, laminating, binding, or compressing of original meat pieces
    • 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
    • A23L13/00—Meat products; Meat meal; Preparation or treatment thereof
    • A23L13/40—Meat products; Meat meal; Preparation or treatment thereof containing additives
    • A23L13/42—Additives other than enzymes or microorganisms in meat products or meat meals
    • A23L13/424—Addition of non-meat animal protein material, e.g. blood, egg, dairy products, fish; Proteins from microorganisms, yeasts or fungi
    • 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
    • A23L13/00—Meat products; Meat meal; Preparation or treatment thereof
    • A23L13/40—Meat products; Meat meal; Preparation or treatment thereof containing additives
    • A23L13/48—Addition of, or treatment with, enzymes
    • 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
    • A23L13/00—Meat products; Meat meal; Preparation or treatment thereof
    • A23L13/50—Poultry products, e.g. poultry sausages
    • A23L13/52—Comminuted, emulsified or processed products; Pastes; Reformed or compressed products from poultry meat
    • 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
    • A23L17/00—Food-from-the-sea products; Fish products; Fish meal; Fish-egg substitutes; Preparation or treatment thereof
    • A23L17/65—Addition of, or treatment with, microorganisms or enzymes
    • 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
    • A23L17/00—Food-from-the-sea products; Fish products; Fish meal; Fish-egg substitutes; Preparation or treatment thereof
    • A23L17/75—Coating with a layer, stuffing, laminating, binding or compressing of original fish pieces
    • 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
    • A23L29/00—Foods or foodstuffs containing additives; Preparation or treatment thereof
    • A23L29/06—Enzymes
    • 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
    • A23L29/00—Foods or foodstuffs containing additives; Preparation or treatment thereof
    • A23L29/20—Foods or foodstuffs containing additives; Preparation or treatment thereof containing gelling or thickening agents
    • A23L29/275—Foods or foodstuffs containing additives; Preparation or treatment thereof containing gelling or thickening agents of animal origin, e.g. chitin
    • A23L29/281—Proteins, e.g. gelatin or collagen

Definitions

  • the invention relates to a method for bonding meat parts by mixing meat parts with a solution comprising fibrinogen and transglutaminase, thrombin and calcium ions as essential components.
  • the invention also relates to the composite meat product which can be obtained with this method.
  • a method according to the preamble is described in the European patent specification EP 0201975.
  • the underlying mechanism of this method is as follows.
  • the protein fibrinogen consists of three subunits A ⁇ , B ⁇ and ⁇ , which are joined by disulphide bonds.
  • Thrombin causes the fibrinopeptides A (18 amino acids) and B (20 amino acids) to be isolated from the amino terminal ends of A ⁇ and B ⁇ .
  • the fibrin monomers having the subunit structure ⁇ ) 2 , spontaneously form aggregates while a weak fibrin gel is formed.
  • the transglutaminase is also activated.
  • transglutaminase forms ⁇ -( ⁇ -glutamyl)l sine crosslinks between the ⁇ -chains of adjacent fibrin monomers and a firmly branched fibrin gel is formed.
  • transglutaminase and casein.
  • transglutaminases coming from microorganisms are used.
  • a disadvantage of the use of microbial transglutaminases is the low substrate specificity. When they penetrate deeper into the meat, proteins in the meat product can be cross-linked further than is desired.
  • An essential factor in bonding meat or fish parts is the strength of the bonding gel layer.
  • the strength of the fibrin gel can be enhanced with a method as mentioned in the preamble, which is characterized in that a reducing agent is added to the solution or a part of the solution of fibrinogen and transglutaminase is replaced by a different protein or a different protein solution.
  • the final concentration of the reducing agent is at least 2 mM.
  • the final concentration of the reducing agent is 2 - 100 mM, more preferably 5 - 25 mM and still more preferably 8 - 12 mM.
  • the reducing agent is preferably added to the solution before raw meat parts are treated with the solution.
  • the reducing agent is preferably selected from cysteine, sulf ⁇ te and peptides or proteins containing one or more cysteines.
  • Food-grade reducing agents are preferred. It will be apparent to the skilled person that the present invention is not to be limited to the above-mentioned reducing agents. Different reducing agents suitable for use in the present invention can also be used.
  • the present invention relates to a method wherein the solution comprises a different protein in an amount of 2 - 40 % by weight in relation to the total of fibrinogen.
  • the solution comprises the other protein in an amount of 5 - 30 % by weight and, more preferably, of 10-25% by weight in relation to the total of fibrinogen.
  • the other protein is a protein containing one or more glutamine and/or lysine residues and contains no intramolecular sulfur bridges.
  • Glutamine and lysine-residues can be covalently bonded by the enzyme transglutaminase. Therefore, it is desired that one or more of these amino acids are present in the other protein. Further, it is not desirable that the other protein has intramolecular disulphide bridges. In case the protein contains cysteines, it is of interest that this amino acid be at a position in the protein such, that it is not possible to form a disulphide bond.
  • proteins usable to this end are casein, casein hydrolysates, myosin, yosin hydrolysates, hemoglobin, globin, collagen, gelatin, whey proteins or soy proteins.
  • the protein is preferably selected from casein, myosin or globin.
  • the reducing agent or the other protein is added in solid form to the existing solution.
  • the reducing agent or the other protein can be added in solution or dispersion to the fibrinogen solution.
  • the reducing agent and the different protein are dissolved or dispersed in a solvent which is selected from water, saline solution or a buffer solution.
  • the above-mentioned solvent has a pH of 5.0 - 9.0, more preferably, however, the above-mentioned solvent has a pH of 7.0 - 8.5.
  • both a reducing agent according to the invention and a different protein according to the invention are added in solid form or in solution or dispersion to the fibrinogen solution according to the preamble.
  • the present invention relates to a method wherein to the solution according to the preamble a fraction containing membranes of erythrocytes is added.
  • a fraction containing membranes of erythrocytes could perform an activating part in the crosslinking of fibrin.
  • adding a fraction containing membranes of erythrocytes to a method as mentioned in the preamble results in a more rapid formation of the fibrin gel. This is probably due to the higher activity of the transglutaminase, so that the fibrin gel is cr ⁇ sslinked more rapidly.
  • the fraction containing membranes of erythrocytes is preferably selected from blood, a fraction with red blood cells, intact erythrocytes and erythrocyte membranes. Intact erythrocytes and erythrocyte membranes can be isolated in a manner known to the skilled person.
  • the above-mentioned fractions are obtained from the same animal the fibrinogen and transglutaminase have been obtained from, but different sources can also be used.
  • both a fraction containing erythrocyte membranes according to the invention, and a reducing agent according to the invention are added in solid form or in solution or dispersion to the fibrinogen solution according to the preamble.
  • the methods according to the invention are preferably carried out at -2 - 40°C, more preferably at 0 - 20°C and still more preferably at 4 - 10°C.
  • one or more substances can be added to the protein solution according to the invention. These substances are, for instance, lactose, maltose, sucrose, maltitol, mannitol, sorbitol, dextrin, branched dextrins, cyclodextrins, glucose, starch, polysaccharides, pectin, oils, fats, gums, emulsifying agents, vitamins, minerals.
  • the methods according to the invention are used for bonding pre-treated or non-pretreated raw meat such as, inter alia, the meat of pigs, cattle, horses, goats, sheep, chickens, rabbits, deer, turkeys and the like but this should not be taken as being limitative.
  • the methods according to the invention can also be used for crosslinking other pretreated or non-pretreated raw food products such as, inter alia, material obtained from fish, crustaceans, snails, frogs legs, worms and insects.
  • the present invention further relates to a composite meat product which can be obtained with one of the methods according to the invention.
  • the present invention relates to a composition for bonding foodstuffs which, in addition to fibrinogen and transglutaminase, contains a reducing agent.
  • the reducing agent is preferably selected from cysteine, sulfite and peptides or proteins containing one or more cysteines. Most preferred is cysteine. Food-grade reducing agents are preferred. It will be apparent to the skilled person that a composition according to the present invention, in addition to the reducing agents mentioned hereinabove, can also contain different suitable reducing agents.
  • the invention also relates to a composition for bonding foodstuffs which comprises fibrinogen and transglutaminase, while 2 - 40% of the fibrinogen has been replaced by a different protein.
  • the other protein is a protein containing one or more glutamine and or lysine residues and no intramolecular sulfur bridges.
  • Glutamine and lysine residues can be covalently bonded by the enzyme transglutaminase. Therefore, it is desired that one or more of these amino acids be present in the other protein. Further, it is not desirable that the different protein has intramolecular disulphide bridges. This is the case when the protein does not contain cysteines. In case the protein does contain cysteines, it is of importance that the amino acids be located in the protein at a position such, that it is not possible to form a disulphide bridge. A different possibility could be to unfold the protein by breaking the disulphide bridges and to keep the protein in a solution wherein this protein remains in unfolded condition. Further, it is desired that this protein is food-grade, so that it can be used without problems in various products.
  • proteins usable to this end are casein, casein hydrolysates, myosin, myosin hydrolysates, hemoglobin, globin, collagen, gelatin, whey proteins or soy proteins.
  • the different protein contains casein, myosin or globin.
  • the invention relates to a composition for bonding foodstuffs which, besides containing fibrinogen and transglutaminase, has a fraction containing erythrocyte membranes.
  • the fraction containing erythrocyte membranes is preferably selected from blood, a fraction with red blood cells, intact erythrocytes and erythrocyte membranes. Intact erythrocytes and erythrocyte membranes can be isolated in a manner known to the skilled person.
  • the above-mentioned fractions are obtained from the same animal the fibrinogen and transglutaminase are obtained from, but other sources can also be used.
  • This reducing agent is preferably selected from the reducing agents enumerated hereinabove.
  • compositions according to the invention are preferably in solid form and can, in addition to the above-mentioned elements, also contain other elements such as, inter aha, lactose, maltose, sucrose, maltitol, mannitol, sorbitol, dextrin, branched dextrins, cyclodextrins, glucose, starch, polysaccharides, pectin, oils, fats, gums, emulsifying agents, vitamins, minerals.
  • other elements such as, inter aha, lactose, maltose, sucrose, maltitol, mannitol, sorbitol, dextrin, branched dextrins, cyclodextrins, glucose, starch, polysaccharides, pectin, oils, fats, gums, emulsifying agents, vitamins, minerals.
  • Example 1 Measurement of the gelling of a solution containing fibrinogen and transglutaminase. thrombin, calcium ions and reducing agent.
  • fibrinogen 5.5 % by weight
  • transglutaminase 250 ⁇ g/ml
  • sulfite cysteine or dithiothreitol (DTT) were dissolved by rolling on a roller bank.
  • the final concentration of the reducing agent was 10 mM.
  • 0.5 ml of a solution of thrombin (20 NIH units/ml) and calcium (0.6 M) was added and briefly and calmly mixed.
  • Example 2 Measurement of the gelling of a solution containing fibrinogen and transglutaminase. thrombin. calcium ions and a different protein.
  • Example 3 Measurement of the gelling of a solution containing fibrinogen and transglutaminase, thrombin, calcium ions, a different protein and a reducing agent.
  • Example 4 Measurement of the gel strength of a solution containing fibrinogen and transglutaminase, thrombin, calcium ions and a fraction with membranes of red blood cells.
  • Fig. 1 shows the measurement of the gel strength of a solution containing fibrinogen and transglutaminase, thrombin and calcium ions with or without a reducing agent. On the x-axis, the time in minutes is indicated and on the y-axis the gel strength G 1 in kPa. The continuous line represents the measurement of the gel strength of a solution of fibrinogen, transglutaminase, thrombin and calcium ions.
  • the interrupted line represents the measurement of the gel strength of a solution of fibrinogen, transglutaminase, thrombin, calcium ions and the reducing agent cysteine and the dotted line represents the measurement of the gel strength of a solution of fibrinogen, transglutaminase, thrombin, calcium ions and the reducing agent sulfite.
  • Fig. 2 shows the measurement of the gel strength of a solution containing fibrinogen and transglutaminase, thrombin, calcium ions with or without another protein.
  • the time in minutes is indicated and on the y-axis the gel strength G' in kPa.
  • the continuous line represents the measurement of the gel strength of a solution of fibrinogen, transglutaminase, thrombin and calcium ions.
  • the dotted line represents the measurement of the gel strength of a solution of fibrinogen, transglutaminase, thrombin, calcium ions and casein.
  • Fig. 3 shows the measurement of the gel strength of a solution containing fibrinogen and transglutaminase, thrombin and calcium ions with or without cysteine and with or without a different protein.
  • the time in minutes is indicated and on the y-axis the gel strength G' in kPa.
  • the continuous line represents the measurement of the gel strength of a solution of fibrinogen, transglutaminase, thrombin, calcium ions and water.
  • the interrupted line represents the measurement of the gel strength of a solution of fibrinogen, transglutaminase, thrombin, calcium ions and casein.
  • the dotted line represents the measurement of the gel strength of a solution of fibrinogen, transglutaminase, thrombin, calcium ions, cysteine and water.
  • the line which is both interrupted and dotted represents the measurement of the gel stren th of a solution of fibrinogen, transglutaminase, thrombin, calcium ions, casein and cysteine.
  • Fig. 4 shows the measurement of the gel strength of a solution which consists of fibrinogen, transglutaminase, thrombin and calcium ions and which can further contain a fraction with red blood cells, a fraction with membranes of red blood cells or a fraction with red blood cells and cysteine.
  • the continuous line represents the measurement of the gel strength of a solution of fibrinogen, transglutaminase, thrombin, calcium ions and a fraction with red blood cells.
  • the dotted line represents the measurement of the gel strength of a solution of fibrinogen, transglutaminase, thrombin, calcium ions and a fraction with red blood cells.
  • the interrupted line represents the measurement of the gel strength of a solution of fibrinogen, transglutaminase, thrombin, calcium ions and a fraction with red blood cells and cystein.
  • the line which is both dotted and interrupted represents the measurement of the gel strength of a solution of fibrinogen, transglutaminase, thrombin and calcium ions (control experiment).

Abstract

L'invention concerne un procédé pour lier de la viande et du poisson. Dans un mode de réalisation, des morceaux de viande ou de poissons sont liés ensemble par mélange dans une solution comprenant du fibrinogène, de la transglutaminase, de la thrombine, des ions de calcium et un agent de réduction. Dans un autre mode de réalisation, des morceaux de viande ou de poissons sont liés ensemble par mélange dans une solution comprenant du fibrinogène, de la transglutaminase, de la thrombine, des ions de calcium et une protéine différente. Dans encore un autre mode de réalisation, des morceaux de viande ou de poissons sont liés ensemble par mélange dans une solution comprenant du fibrinogène, de la transglutaminase, de la thrombine, des ions de calcium et une fraction composée d'éléments de globules rouges. La présente invention porte également sur le produit composite à base de viande obtenu selon les procédés susmentionnés, ainsi que sur des compositions contenant du fibrinogène, de la transglutaminase et une protéine différente ou une fraction composée d'éléments de globules rouges et/ou un agent de réduction.
PCT/NL2002/000293 2001-05-04 2002-05-03 Procédé pour lier de la viande et du poisson WO2002089607A1 (fr)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
NL1017994 2001-05-04
NL1017994A NL1017994C2 (nl) 2001-05-04 2001-05-04 Hechting van vlees- en visproducten.

Publications (1)

Publication Number Publication Date
WO2002089607A1 true WO2002089607A1 (fr) 2002-11-14

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Citations (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0201975A1 (fr) * 1985-05-09 1986-11-20 Nederlandse Organisatie voor toegepast-natuurwetenschappelijk onderzoek TNO Produit de viande composé et son procédé de préparation
EP0572987A2 (fr) * 1992-06-02 1993-12-08 Ajinomoto Co., Inc. Préparation enzymatique et procédé pour fabriquer un produit alimentaire formé lié
EP0686401A2 (fr) * 1994-06-10 1995-12-13 Ajinomoto Co., Inc. Colle pour tissu vivant et coagulant sanguin
WO1998043686A1 (fr) * 1997-04-03 1998-10-08 California Institute Of Technology Modification enzymatique de la fibrine destinee au genie tissulaire
DE19853033A1 (de) * 1998-11-18 2000-05-25 Centeon Pharma Gmbh Stabilisierte Proteinzubereitung für einen Gewebekleber
US6221405B1 (en) * 1999-05-11 2001-04-24 Jac Pac Foods, Ltd. Method of bonding and tenderizing meat

Patent Citations (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0201975A1 (fr) * 1985-05-09 1986-11-20 Nederlandse Organisatie voor toegepast-natuurwetenschappelijk onderzoek TNO Produit de viande composé et son procédé de préparation
EP0572987A2 (fr) * 1992-06-02 1993-12-08 Ajinomoto Co., Inc. Préparation enzymatique et procédé pour fabriquer un produit alimentaire formé lié
EP0686401A2 (fr) * 1994-06-10 1995-12-13 Ajinomoto Co., Inc. Colle pour tissu vivant et coagulant sanguin
WO1998043686A1 (fr) * 1997-04-03 1998-10-08 California Institute Of Technology Modification enzymatique de la fibrine destinee au genie tissulaire
DE19853033A1 (de) * 1998-11-18 2000-05-25 Centeon Pharma Gmbh Stabilisierte Proteinzubereitung für einen Gewebekleber
US6221405B1 (en) * 1999-05-11 2001-04-24 Jac Pac Foods, Ltd. Method of bonding and tenderizing meat

Non-Patent Citations (1)

* Cited by examiner, † Cited by third party
Title
JANSSEN A G W: "Marktvertrouwen in vleeshechter groeit", VOEDINGSMIDDELEN TECHNOLOGIE, NOORDERVLIET B.V. ZEIST, NL, vol. 29, no. 14/15, 11 July 1996 (1996-07-11), pages 31, XP002101383, ISSN: 0042-7934 *

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