EP1406508A1 - Systeme d'hydrolyse de proteines - Google Patents

Systeme d'hydrolyse de proteines

Info

Publication number
EP1406508A1
EP1406508A1 EP00984612A EP00984612A EP1406508A1 EP 1406508 A1 EP1406508 A1 EP 1406508A1 EP 00984612 A EP00984612 A EP 00984612A EP 00984612 A EP00984612 A EP 00984612A EP 1406508 A1 EP1406508 A1 EP 1406508A1
Authority
EP
European Patent Office
Prior art keywords
meal
animal
meat
bone meal
pathogens
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Withdrawn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
EP00984612A
Other languages
German (de)
English (en)
Inventor
Ernst Kager
Volker Dr. Wagner
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.)
Individual
Original Assignee
Individual
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 Individual filed Critical Individual
Publication of EP1406508A1 publication Critical patent/EP1406508A1/fr
Withdrawn legal-status Critical Current

Links

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
    • A23J1/001—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from waste materials, e.g. kitchen waste
    • A23J1/002—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from waste materials, e.g. kitchen waste from animal waste materials
    • 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
    • A23J1/10—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from hair, feathers, horn, skins, leather, bones, or the like
    • 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
    • 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
    • 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
    • A23J3/341—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of animal proteins
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23K—FODDER
    • A23K20/00—Accessory food factors for animal feeding-stuffs
    • A23K20/10—Organic substances
    • A23K20/142—Amino acids; Derivatives thereof
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23K—FODDER
    • A23K20/00—Accessory food factors for animal feeding-stuffs
    • A23K20/10—Organic substances
    • A23K20/142—Amino acids; Derivatives thereof
    • A23K20/147—Polymeric derivatives, e.g. peptides or proteins

Definitions

  • the invention relates to a plant which separates proteins, such as those present in animal meal, animal blood meal and animal bone meal, into amino acids by dissolving them in acidic or basic solution. By subsequent neutralization (pH neutral) and drying, a prion-free solid is obtained from the liquid.
  • proteins such as those present in animal meal, animal blood meal and animal bone meal
  • the pathogen of Creutzfeldt-Jakobs disease which is biologically practically identical to the BSE pathogen, thus becomes a great risk for humans.
  • the pathogen of prion diseases the so-called prion, is a completely new type of pathogen that differs from bacteria and the viruses known to date in essential points: prions are extremely resistant to heat and chemicals. Even heating to 100 degrees C cannot inactivate prions, and many of the common disinfectants have little effect. Prions are also very difficult to biodegrade - they survive in the earth for years.
  • a protein can be identified in the infected brain, which is only observed specifically in prion diseases.
  • This protein the "scrapie prion protein", PrPSc for short (also called PrPBSE in BSE), is a modified form of the prion protein PrPC, which is found in the normal body.
  • PrPSc is resistant to digestive enzyme breakdown (digestive enzymes are proteins that digest food in the human stomach, for example), while PrPC is completely destroyed by treatment with digestive enzymes.
  • PrPSc is a component of prion, the pathogen of prion diseases.
  • PrPSc itself represents the whole pathogen.
  • PrPSc converts PrPC to PrPSc.
  • PrPSc can in turn now The principle is based on the chemical breakdown of the proteins into their individual parts, the amino acids. This method means that no information and therefore no disease can be transmitted or triggered.
  • amino acids 20 different amino acids are involved in the construction of the proteins.
  • sequence of these amino acids in proteins is called the amino acid sequence and describes it as the primary structure.
  • This primary structure can be destroyed by hydrolysis / cleavage in aqueous solution by adding acids or alkalis as well as possibly proteases (such as trypsin, chymotrypsin, pepsin, papain, subtilisin, elastase and thermolysin).
  • acids or alkalis as well as possibly proteases (such as trypsin, chymotrypsin, pepsin, papain, subtilisin, elastase and thermolysin).
  • the proteins are broken down into their individual components, the individual amino acids.
  • the spatial structure (secondary, tertiary and quaternary structure) is of course lost, and with it all information and harmful effects associated with this.
  • the protein involved in the disease BSE is also broken down into its components and can therefore no longer develop its harmful effects.
  • the animal meal, animal blood meal and animal bone meal are dissolved in either basic (pH value> 11; added hydroxide e.g. sodium hydroxide) or acidic (added acid e.g. with hydrochloric acid; pH ⁇ 1) water.
  • added hydroxide e.g. sodium hydroxide
  • acidic e.g. with hydrochloric acid; pH ⁇ 1
  • This process can also be supported by the further addition of enzymes (e.g. trypsin) or heat (heating to e.g. 37 degrees Celsius).
  • enzymes e.g. trypsin
  • heat heating to e.g. 37 degrees Celsius
  • the solution is neutralized with the amino acids (pH neutral by adding basic or acidic neutralizing agents) and the amino acids are recovered as a solid by drying.
  • This solid can then be used in agriculture instead of today's animal meal, animal blood meal and animal bone meal (e.g. as an animal feed additive).

Landscapes

  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Polymers & Plastics (AREA)
  • Food Science & Technology (AREA)
  • Engineering & Computer Science (AREA)
  • Zoology (AREA)
  • Biochemistry (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Health & Medical Sciences (AREA)
  • Nutrition Science (AREA)
  • Animal Husbandry (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • General Chemical & Material Sciences (AREA)
  • Fodder In General (AREA)
  • Peptides Or Proteins (AREA)

Abstract

Le nombre croissant de cas d'ESB chez les bovins ces dernières années est lié à la présence de farines animales, de farines de sang animal et de farines d'os animaux dans la nourriture donnée au bétail. Les déchets d'abattage de moutons (pathogènes de la tremblante du mouton), de chèvres (pathogènes de la tremblante du mouton) et de bovins (pathogènes de l'ESB) sont transformés en farines animales, farines de sang animal et farines d'os animaux et sont donnés à manger aux bovins. Tous les procédés de production de farines animales, de farines de sang animal et de farines d'os animaux utilisés en Europe se sont avérés peu fiables en matière de destruction des agents pathogènes et donc de protection contre la transmission de la maladie (ESB). Selon ces procédés, la matière première (déchets et cadavres d'animaux) est broyée, chauffée et séchée. Après extraction de la graisse, la matière est réduite en farine d'os. Les températures de stérilisation appliquées ne permettent cependant pas de détruire les agents pathogènes. Des farines de viande et d'os infectieuses, de même que de la graisse animale infectieuse se retrouvent ainsi dans le cycle alimentaire des animaux. Des farines animales, des farines de sang animal et des farines d'os animaux sont données à manger aux bovins, aux porcs, aux ovins, aux volailles et aux poissons d'élevage. Le procédé selon l'invention et la procédure employée font appel à un nouveau principe de destruction et d'élimination des protéines présentes dans les farines animales, les farines de sang animal et les farines d'os animaux et, par là même, des agents pathogènes des maladies du prion. Ce principe repose sur la décomposition chimique des protéines en leurs constituants, les acides aminés. Grâce à cette procédure, plus aucune information ne peut être transmise et donc plus aucune maladie ne peut se déclarer. La protéine impliquée dans l'ESB est également décomposée en ses constituants et ne peut donc plus déployer son action néfaste. Après décomposition totale, la solution contenant les acides aminés est neutralisée (pH rendu neutre par addition d'agents de neutralisation basiques ou acides) et les acides aminés sont récupérés sous forme de matière solide par séchage. Cette matière solide peut être ensuite employée dans l'agriculture à la place des farines animales, des farines de sang animal et des farines d'os animaux actuelles (p. ex. comme compléments alimentaires).
EP00984612A 2000-12-21 2000-12-21 Systeme d'hydrolyse de proteines Withdrawn EP1406508A1 (fr)

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
PCT/AT2000/000348 WO2002049449A1 (fr) 2000-12-21 2000-12-21 Systeme d'hydrolyse de proteines

Publications (1)

Publication Number Publication Date
EP1406508A1 true EP1406508A1 (fr) 2004-04-14

Family

ID=3619079

Family Applications (1)

Application Number Title Priority Date Filing Date
EP00984612A Withdrawn EP1406508A1 (fr) 2000-12-21 2000-12-21 Systeme d'hydrolyse de proteines

Country Status (2)

Country Link
EP (1) EP1406508A1 (fr)
WO (1) WO2002049449A1 (fr)

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2006069803A1 (fr) 2004-12-23 2006-07-06 Animox Gmbh Procede de production d'hydrolysats proteiques

Family Cites Families (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE2756739C2 (de) * 1977-12-20 1983-11-24 Röhm GmbH, 6100 Darmstadt Verfahren zum Aufarbeiten von Tierkörper-, Knochen- und Fleischabfällen
CN1098260A (zh) * 1994-02-03 1995-02-08 商业部食品检测科学研究所 一种从动物骨骼中提取酶水解蛋白质方法
FR2751177B1 (fr) * 1996-07-17 1998-08-28 Morelle Jean Compositions exemptes de proteines et de peptides obtenues a partir de toutes proteines animales, destinees a l'alimentation animale et humaine, ainsi qu'a l'usage cosmetique pharmaceutique et agricole
EP1021958A1 (fr) * 1999-01-25 2000-07-26 S.I.C.IT. S.p.A. Procédé d'hydrolyse chimique sur des bouillons protéiques, déchets d'origine animale et résidus organiques animaux

Non-Patent Citations (1)

* Cited by examiner, † Cited by third party
Title
See references of WO0249449A1 *

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2006069803A1 (fr) 2004-12-23 2006-07-06 Animox Gmbh Procede de production d'hydrolysats proteiques
US8759497B2 (en) 2004-12-23 2014-06-24 Animox Gmbh Method for producing protein hydrolysates

Also Published As

Publication number Publication date
WO2002049449A1 (fr) 2002-06-27

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