EP1406508A1 - Protein hydrolysis system - Google Patents

Protein hydrolysis system

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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.)
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Application number
EP00984612A
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German (de)
French (fr)
Inventor
Ernst Kager
Volker Dr. Wagner
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Individual
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Individual
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Publication of EP1406508A1 publication Critical patent/EP1406508A1/en
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Classifications

    • AHUMAN NECESSITIES
    • A23FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23JPROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J1/00Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
    • A23J1/001Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from waste materials, e.g. kitchen waste
    • A23J1/002Obtaining 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
    • AHUMAN NECESSITIES
    • A23FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23JPROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J1/00Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
    • A23J1/10Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from hair, feathers, horn, skins, leather, bones, or the like
    • AHUMAN NECESSITIES
    • A23FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23JPROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J3/00Working-up of proteins for foodstuffs
    • A23J3/04Animal proteins
    • AHUMAN NECESSITIES
    • A23FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23JPROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J3/00Working-up of proteins for foodstuffs
    • A23J3/30Working-up of proteins for foodstuffs by hydrolysis
    • A23J3/32Working-up of proteins for foodstuffs by hydrolysis using chemical agents
    • AHUMAN NECESSITIES
    • A23FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23JPROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J3/00Working-up of proteins for foodstuffs
    • A23J3/30Working-up of proteins for foodstuffs by hydrolysis
    • A23J3/32Working-up of proteins for foodstuffs by hydrolysis using chemical agents
    • A23J3/34Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes
    • A23J3/341Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of animal proteins
    • AHUMAN NECESSITIES
    • A23FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23KFODDER
    • A23K20/00Accessory food factors for animal feeding-stuffs
    • A23K20/10Organic substances
    • A23K20/142Amino acids; Derivatives thereof
    • AHUMAN NECESSITIES
    • A23FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23KFODDER
    • A23K20/00Accessory food factors for animal feeding-stuffs
    • A23K20/10Organic substances
    • A23K20/142Amino acids; Derivatives thereof
    • A23K20/147Polymeric 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)
  • Nutrition Science (AREA)
  • Health & Medical Sciences (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • General Chemical & Material Sciences (AREA)
  • Animal Husbandry (AREA)
  • Peptides Or Proteins (AREA)
  • Fodder In General (AREA)

Abstract

The increasing number of BSE diseases in cattle in recent years is associated with feeding animals meat meal, animal blood meal and animal bone meal. Slaughterhouse wastes from sheep (scrapie pathogens), goats (scrapie pathogens) and from cattle (BSE pathogens) are processed into meat meal, animal blood meal and into animal bone meal and are then fed to cattle. All methods used in Europe for producing meat meal, animal blood meal and animal bone meal have been proven unreliable in destroying the pathogens and thus in providing protection against the transmission of the disease (BSE). In these methods, the raw material (animal cadavers and wastes) are comminuted, heated and dried. After pressing out the fat, the material is ground into bone meal. The temperatures used for sterilizing are, however, incapable of destroying the pathogen. As a result, infectious meat-and-bone meal as well as infectious animal fat enter the feed cycle. Meat meal, animal blood meal and animal bone meal are fed to cattle, pigs, sheep, poultry and cultivated fish. The inventive method and the procedure provide a novel approach to destroying and eradicating the proteins contained in the meat meal, animal blood meal and animal bone meal and, with them, the pathogens of prion diseases. The principle is based on the chemical breakdown of the proteins into their individual parts: amino acids. Thanks to this procedure, information can no longer be transferred thereby preventing the triggering of disease. In addition, the protein involved in the disease BSE is broken down into its constituents and can no longer unleash its harmful effect. After decomposition is complete, the solution is neutralized with amino acids (rendered pH neutral by adding alkaline or acid neutralizing agents), and the amino acids are recovered as solid matter by drying. This solid matter can be used in agriculture (e.g. as an animal feed supplement) in place of present day meat meal, animal blood meal and animal bone meal.

Description

Beschreibung description
EiweisshydrolyseanlageEiweisshydrolyseanlage
Die Erfindung betrifft eine Anlage die Proteine, wie sie in Tiermehl, Tierblutmehl sowie Tierknochenmehl vorhanden sind, durch Auflösen in saurer oder basischer Lösung in Aminosäuren auftrennt. Durch anschließende Neutralisation (pH-neutral) und Trocknung wird aus der Flüssigkeit ein prionenfreier Feststoff gewonnen.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.
Die steigende Zahl von BSE-Erkrankungen bei Rindern in den letzten Jahren wird mit der Verfütterung von Tiermehl, Tierblutmehl sowie Tierknochenmehl in Verbindung gebracht. Schlachtabfälle von Schafen (Scrapie-Erreger), Ziegen (Scrapie-Erreger) sowie von Rindern (BSE-Erreger) werden zu Tiermehl, Tierblutmehl sowie Tierknochenmehl verarbeitet und an Rinder verfüttert.The increasing number of BSE diseases in cattle in recent years has been linked to the feeding of animal meal, animal blood meal and animal bone meal. Slaughter waste from sheep (scrapie pathogen), goat (scrapie pathogen) and cattle (BSE pathogen) are processed into animal meal, animal blood meal and animal bone meal and fed to cattle.
Alle in Europa angewendeten Verfahren zur Tiermehl-, Tierblutmehl- sowie Tierknochenmehl-Herstellung sind erwiesenermaßen nicht sicher, um die Erreger abzutöten und so einen Schutz gegen die Übertragung der Krankheit (BSE) zu bewirken. Bei diesen Verfahren wird das Rohmaterial (Tierkadaver und Abfälle) zerkleinert, erhitzt und getrocknet. Nach Abpressen des Fettes wird das Material zu Knochenmehl gemahlen. Die dabei zur Sterilisation aufgewendeten Temperaturen sind jedoch nicht in der Lage, den Erreger zu zerstören. Somit kommt infektiöses Fleischknochenmehl und ebenfalls infektiöses Tierfett in den Futterkreislauf. Tiermehl, Tierblutmehl sowie Tierknochenmehl wird an Rinder, Schweine, Schafe, Geflügel und Zuchtfische verfüttert.All methods used in Europe for the production of animal meal, animal blood meal and animal bone meal are proven to be unsafe to kill the pathogens and thus provide protection against the transmission of the disease (BSE). In this process, the raw material (animal carcasses and waste) is crushed, heated and dried. After pressing the fat, the material is ground to bone meal. However, the temperatures used for sterilization are not able to destroy the pathogen. Infectious meat bone meal and also infectious animal fat thus enter the feed cycle. Animal meal, animal blood meal and animal bone meal are fed to cattle, pigs, sheep, poultry and farmed fish.
Der biologisch praktisch mit dem BSE-Erreger idente Erreger der Creutzfeldt-Jakobs- Krankheit wird somit zum großen Risiko für den Menschen. Bei dem Krankheitserreger der Prionenerkrankungen, dem sogenannten Prion, handelt es sich um eine völlig neue Art von Erreger, der sich von Bakterien und den bis heute bekannten Viren in wesentlichen Punkten unterscheidet: Prionen sind extrem resistent gegen Hitze und Chemikalien. Selbst Erhitzen auf 100 Grad C kann Prionen nicht inaktivieren, und viele der gebräuchlichen Desinfektionsmittel zeigen kaum Wirkung. Prionen sind auch nur sehr schwer biologisch abbaubar - in der Erde überleben sie über Jahre hinweg.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.
Im infizierten Gehirn lässt sich ein Protein identifizieren, welches spezifisch nur bei Prionenerkrankungen beobachtet wird. Dieses Protein, das "Scrapie Prionprotein", kurz PrPSc (bei BSE auch PrPBSE genannt), ist eine abgewandelte Form des im normalen Körper vorkommenden Prionproteins PrPC.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.
Die beiden Proteine, das krankheitsspezifische PrPSc und das normale PrPC unterscheiden sich durch ihre unterschiedliche räumliche Struktur. Ein weiterer Unterschied besteht darin, dass PrPSc resistent ist gegen den Abbau durch Verdauungsenzyme (Verdauungsenzyme sind Proteine die z.B. im menschlichen Magen die Nahrung verdauen), während PrPC durch Behandlung mit Verdauungsenzymen vollständig zerstört wird.The two proteins, the disease-specific PrPSc and the normal PrPC differ in their different spatial structure. Another difference is that 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.
Auf Grund vieler Studien ist die Wissenschaft heute zur Schlussfolgerung gekommen, dass PrPSc ein Bestandteil des Prions, des Krankheitserregers der Prionenerkrankungen ist. Man spekuliert sogar, dass PrPSc selbst den ganzen Erreger darstellt. Nach dieser Theorie bewirkt bei einer Infektion das eindringende PrPSc eine Umwandlung von PrPC in PrPSc. Das neu entstandene PrPSc kann nun seinerseits die Das Prinzip beruht auf der chemischen Zerlegung der Proteine (Eiweiße) in ihre Einzelteile, die Aminosäuren. Durch diese Methode können keine Information und somit keine Krankheit mehr übertragen bzw. ausgelöst werden.Based on many studies, science has come to the conclusion today that PrPSc is a component of prion, the pathogen of prion diseases. One even speculates that PrPSc itself represents the whole pathogen. According to this theory, when an infection occurs, the invading PrPSc converts PrPC to PrPSc. The newly created 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.
Die Methode wird in Abbildung 1 dargestellt und wirkt wie folgt:The method is shown in Figure 1 and works as follows:
Am Aufbau der Proteine sind 20 verschiedene Aminosäuren beteiligt. Die Abfolge dieser Aminosäuren in Proteinen nennt man Aminosäuresequenz und beschreibt sie als Primärstruktur.20 different amino acids are involved in the construction of the proteins. The sequence of these amino acids in proteins is called the amino acid sequence and describes it as the primary structure.
Diese Primärstruktur kann durch Hydrolyse/Spaltung in wässriger Lösung durch Zugabe von Säuren oder Laugen sowie eventuell Proteasen (wie z.B. Trypsin, Chymotrypsin, Pepsin, Papain, Subtilisin, Elastase und Thermolysin) zerstört werden.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).
Hierbei werden die Proteine in ihre Einzelbestandteile, die einzelnen Aminosäuren, zerlegt. Neben der Primärstrukutr geht hierbei natürlich auch die räumliche Struktur (Sekundär-, Tertiär- und Quartärstruktur) verloren und somit jegliche hiermit verbundene Information und schädliche Auswirkungen.The proteins are broken down into their individual components, the individual amino acids. In addition to the primary structure, the spatial structure (secondary, tertiary and quaternary structure) is of course lost, and with it all information and harmful effects associated with this.
Auch das bei der Krankheit BSE beteiligte Protein wird in seine Bestandteile zerlegt und kann somit nicht mehr seine schädliche Wirkung entfalten.The protein involved in the disease BSE is also broken down into its components and can therefore no longer develop its harmful effects.
Eine dafür benötigte Anlage wird wie folgt aussehen (Abbildung 2):A system required for this will look as follows (Figure 2):
Das Tiermehl, Tierblutmehl sowie Tierknochenmehl wird in entweder basischem (pH-Wert > 11 ; Hydroxidzusatz z.Bspl. Natriumhydroxid) oder saurem (Säurezusatz z.B. mit Salzsäure ; pH-Wert < 1 ) Wasser aufgelöst. In dieser Umgebung werden die Ketten der Proteine gespalten und in einzelne Aminosäuren aufgelöst.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. In this environment, the chains of proteins are split and broken down into individual amino acids.
Dieser Prozess kann auch durch die weitere Zugabe von Enzymen (zB. Trypsin) oder Wärme (erhitzen auf z.B. 37 Grad Celsius) unterstützt werden.This process can also be supported by the further addition of enzymes (e.g. trypsin) or heat (heating to e.g. 37 degrees Celsius).
Die vollständige Aufspaltung der Aminosäureketten in einzelne Aminosäuren wird nach diesem Vorgang mittels Analyse kontrolliert (z.B. durch Aminosäureanalysatoren).After this process, the complete splitting of the amino acid chains into individual amino acids is checked by analysis (e.g. by amino acid analyzers).
Nach der vollständigen Aufspaltung wird die Lösung mit den Aminosäuren neutralisiert (pH- neutral durch Zusetzen von basischen oder sauren Neutralisationsmitteln) und die Aminosäuren durch Trocknen als Feststoff zurückgewonnen. Dieser Feststoff kann dann anstelle des heutigen Tiermehls, Tierblutmehls sowie Tierknochenmehls in der Landwirtschaft eingesetzt werden (z.B. als Tierfutterzusatz). After complete splitting, 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).

Claims

EiweißhydrolyseanlagePatentansprüche EiweißhydrolyseanlagePatentansprüche
1.) Eine Anlage, die dadurch gekennzeichnet ist, dass Proteine, wie sie in Tiermehl, Tierblutmehl sowie Tierknochenmehl vorhanden sind, durch Auflösen in saurer oder basischer Lösung in Aminosäuren aufgetrennt und durch Neutralisation (pH-neutral) und Trocknung zu prionenfreien Feststoffen umgewandelt werden.1.) A system which is characterized in that proteins such as those present in animal meal, animal blood meal and animal bone meal are separated into amino acids by dissolving them in acidic or basic solution and converted to prion-free solids by neutralization (pH-neutral) and drying ,
2.) Eine Anlage wie in Anspruch 1, die dadurch gekennzeichnet ist, dass zusätzlich Proteasen (z.B. Trypsin, Chymotrypsin, Pepsin, Papain, Subtilisin, Elastase und Thermolysin) zur Aufspaltung eingesetzt werden.2.) A system as in claim 1, which is characterized in that proteases (e.g. trypsin, chymotrypsin, pepsin, papain, subtilisin, elastase and thermolysin) are used for the splitting.
3.) Eine Anlage wie in Anspruch 1 , die dadurch gekennzeichnet ist, dass Energie in Form von Wärme (z.Bspl: erhitzen auf 37 Grad C) zugeführt wird.3.) A system as in claim 1, which is characterized in that energy in the form of heat (for example: heating to 37 degrees C) is supplied.
4.) Eine Anlage wie in Anspruch 1, die dadurch gekennzeichnet ist, dass sie mit Hilfe von analytischen Kontrollen die vollständige Aufspaltung der Aminosäureketten nachweist.4.) A plant as in claim 1, which is characterized in that it uses analytical controls to demonstrate the complete splitting of the amino acid chains.
5.) Eine Anlage wie in Anspruch 1, die dadurch gekennzeichnet ist, dass nach einer pH- Wert Einstellung durch Zusetzen von basischen oder sauren Substanzen und einer Kontrolle eine pH-neutrale Lösung mit Aminosäuren entsteht.5.) A system as in claim 1, which is characterized in that after a pH adjustment by adding basic or acidic substances and a control, a pH-neutral solution with amino acids is formed.
6.) Eine Anlage wie in Anspruch 1 , die dadurch gekennzeichnet ist, dass nach Trocknung der ph-neutralen Lösung ein Feststoff entsteht, der prionenfrei ist. 6.) A system as in claim 1, which is characterized in that after drying the pH-neutral solution, a solid is formed which is prion-free.
EP00984612A 2000-12-21 2000-12-21 Protein hydrolysis system Withdrawn EP1406508A1 (en)

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Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2006069803A1 (en) 2004-12-23 2006-07-06 Animox Gmbh Method for producing protein hydrolysates

Family Cites Families (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE2756739C2 (en) * 1977-12-20 1983-11-24 Röhm GmbH, 6100 Darmstadt Process for the processing of carcass, bone and meat waste
CN1098260A (en) * 1994-02-03 1995-02-08 商业部食品检测科学研究所 A kind of from animal skeleton method for extracting enzymatic protein
FR2751177B1 (en) * 1996-07-17 1998-08-28 Morelle Jean COMPOSITIONS FREE OF PROTEINS AND PEPTIDES OBTAINED FROM ANY ANIMAL PROTEINS, INTENDED FOR ANIMAL AND HUMAN FEEDING, AS WELL AS FOR PHARMACEUTICAL AND AGRICULTURAL COSMETIC USE
EP1021958A1 (en) * 1999-01-25 2000-07-26 S.I.C.IT. S.p.A. Chemical hydrolysis of proteinaceous broth, animal waste material and waste material from animal organs

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 (en) 2004-12-23 2006-07-06 Animox Gmbh Method for producing protein hydrolysates
US8759497B2 (en) 2004-12-23 2014-06-24 Animox Gmbh Method for producing protein hydrolysates

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