EP3780967A1 - Verfahren zur gewinnung eines peptidhydrolysats aus tierischen blutproteinen und auf diese weise gewonnenes peptidhydrolysat - Google Patents

Verfahren zur gewinnung eines peptidhydrolysats aus tierischen blutproteinen und auf diese weise gewonnenes peptidhydrolysat

Info

Publication number
EP3780967A1
EP3780967A1 EP19716444.5A EP19716444A EP3780967A1 EP 3780967 A1 EP3780967 A1 EP 3780967A1 EP 19716444 A EP19716444 A EP 19716444A EP 3780967 A1 EP3780967 A1 EP 3780967A1
Authority
EP
European Patent Office
Prior art keywords
blood
hydrolysis
carried out
peptide
peptides
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.)
Pending
Application number
EP19716444.5A
Other languages
English (en)
French (fr)
Inventor
Ludivine SION
Rémi PRZYBYLSKI
Pascal Dhulster
Naïma NEDJAR
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.)
SARIA
Original Assignee
Saria Industries SAS
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 Saria Industries SAS filed Critical Saria Industries SAS
Publication of EP3780967A1 publication Critical patent/EP3780967A1/de
Pending 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
    • A23J1/06—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from blood
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23B—PRESERVATION OF FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES; CHEMICAL RIPENING OF FRUIT OR VEGETABLES
    • A23B2/00—Preservation of foods or foodstuffs, in general
    • A23B2/70—Preservation of foods or foodstuffs, in general by treatment with chemicals
    • A23B2/725—Preservation of foods or foodstuffs, in general by treatment with chemicals in the form of liquids or solids
    • A23B2/729—Organic compounds; Microorganisms; Enzymes
    • A23B2/733—Compounds of undetermined constitution obtained from animals or plants
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23B—PRESERVATION OF FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES; CHEMICAL RIPENING OF FRUIT OR VEGETABLES
    • A23B4/00—Preservation of meat, sausages, fish or fish products
    • A23B4/14—Preserving with chemicals not covered by groups A23B4/02 or A23B4/12
    • A23B4/18—Preserving with chemicals not covered by groups A23B4/02 or A23B4/12 in the form of liquids or solids
    • A23B4/20—Organic compounds; Microorganisms; Enzymes
    • 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
    • A23J3/345—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of animal proteins of blood proteins
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23K—FODDER
    • A23K10/00—Animal feeding-stuffs
    • A23K10/10—Animal feeding-stuffs obtained by microbiological or biochemical processes
    • A23K10/14—Pretreatment of feeding-stuffs with enzymes
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23K—FODDER
    • A23K10/00—Animal feeding-stuffs
    • A23K10/20—Animal feeding-stuffs from material of animal origin
    • A23K10/24—Animal feeding-stuffs from material of animal origin from blood
    • 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
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23K—FODDER
    • A23K50/00—Feeding-stuffs specially adapted for particular animals
    • A23K50/40—Feeding-stuffs specially adapted for particular animals for carnivorous animals, e.g. cats or dogs
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P21/00—Preparation of peptides or proteins
    • C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products

Definitions

  • the present invention relates to a process for obtaining a peptide hydrolyzate from slaughterhouse blood proteins and a peptide hydrolyzate obtained by such a process.
  • peptide hydrolysates derived from hemoglobin have been demonstrated. These include opioid, antihypertensive, analgesic, bradykinin potentiating, hematopoietic, coronary-constrictor, bacterial growth stimulating, lipid-lowering activities (Nedjar-Arroume, et al., 2008. Peptides, 29, 969-977).
  • peptide hydrolysates derived from blood could potentially be used in many fields, for example in the food, as a preservative, or therapeutic or nutraceutical, as an alternative to antibiotics, especially in animal nutrition, but also as active substances intended to destroy, repel or render harmless the pests, to prevent their action or to combat them in agriculture.
  • the nucleic acids likely to be obtained from poultry blood can find applications in pharmacy, in cosmetics, in nutrition and in the field of diagnostics.
  • the methods for obtaining peptide blood hydrolysates of the state of the art involve, after blood collection, a separation step of the plasma and the cruor.
  • the cruor which is almost exclusively composed of hemoglobin, is preserved and the hemoglobin it contains is then subjected to enzymatic digestion using an enzyme, for example porcine pepsin.
  • Some methods of the state of the art also propose to extract hemoglobin from red blood cells by hemolysis. After enzymatic digestion, a fraction enriched in peptides is obtained. At the end of this process, the peptide fraction obtained has a coloration identical to that of the cruor.
  • the solutions or products obtained from the blood are strongly colored by the heme carried by the hemoglobin.
  • the presence of colored compounds is undesirable and incompatible with the applications of the peptide hydrolysates envisaged, in particular when it is envisaged to use them as preservatives or to destine them to food or therapy.
  • the iron contained in Theme activates the oxidation of food in the formulations.
  • the presence of the molecules responsible for this coloration gives an undesirable taste and odor.
  • an object of the present invention is to provide a standardized and controlled process for obtaining a peptide hydrolyzate from blood, which is eco-responsible, ecological and economic, so as to maximize the value of blood, and thanks to which the peptide hydrolysates obtained are both functional in terms of biological activities, such as those mentioned above, and directly usable in any kind of industry, or for any food, agri-food, agricultural, therapeutic or nutraceutical application, and which to do this, does not present staining phenomena.
  • the invention relates to a process for obtaining a peptide hydrolyzate from animal blood, comprising obtaining blood, adding an anticoagulant, an enzymatic hydrolysis reaction, stopping the hydrolysis reaction, the decolorization of the hydrolysis product and the separation of the hydrolysis product into a fraction containing a peptide hydrolyzate and a fraction containing the subject.
  • the process according to the invention is characterized in that the whole blood obtained is introduced into a reactor inside which all of the enzymatic hydrolysis and decolorization reactions are carried out, at ambient temperature, the enzymatic hydrolysis reaction.
  • the method according to the invention meets the expected objectives.
  • peptide hydrolyzate resulting from proteins of blood having a constant composition in peptides, devoid of heme or residues of heme susceptible of give it a color.
  • the peptides have biological activities, in particular opioids, antihypertensives, analgesics, potentiators of bradykinin, hematopoietic, coronaromotive, bacterial growth stimulation, lipid-lowering, such as those described in the state of the art.
  • the method is carried out on whole blood, as collected in slaughterhouses, that is to say without separation of plasma and cruor, or extraction of hemoglobin by hemolysis of red blood cells.
  • This characteristic of the process contributes to the eco-responsibility characteristic since it uses the totality of the raw material. It makes it possible to obtain a hydrolyzate enriched with peptides not only derived from hemoglobin but also from plasma proteins.
  • anticoagulant such as citrate or sodium phosphate, makes this raw material homogeneous and also prevents the loss of material by coagulation phenomena.
  • the enzymatic hydrolysis step is carried out at ambient temperature at an acidic pH, preferably between 3 and 4, so as to preserve the homogeneous medium, without precipitation of the heme, with complete hydrolysis of the proteins and chains. alpha and beta hemoglobin without loss of peptides.
  • Stopping the hydrolysis is done in an alkaline medium by adding base to a basic pH, preferably between 8.5 and 10, in order to irreversibly inactivate the enzyme and to maintain a homogeneous medium.
  • the bleaching step does not involve organic solvents, membranes, adsorbents, bleaches, high pressure treatments, or other complex intermediate step that can reduce the yield of peptides.
  • This step is carried out in a simple and effective manner, by lowering the pH to an acidic value, preferably between 4 and 5. During this step, 100% of the theme is precipitated and all the peptides obtained at the end of the hydrolysis is preserved.
  • the separation of the products of the hydrolysis is carried out by a physical separation method of the type known to those skilled in the art.
  • the peptide hydrolyzate fraction obtained at the end of the process contains more than 99.9% peptides and less than 0.1% heme.
  • the fraction enriched in peptides is directly recoverable. It can be advantageously neutralized, demineralised, concentrated, dried at low temperature and / or lyophilized if necessary.
  • the whole blood is blood of porcine, bovine, ovine, equine, rabbit or avian origin, poultry, or a mixture, preferably bovine or porcine blood.
  • this mixture is for example composed of 70% of bovine blood and 30% of pig blood.
  • the enzyme used during the enzymatic hydrolysis step is an active proteolytic enzyme at acidic pH, preferably porcine pepsin.
  • porcine pepsin EC 3.4.23.1 (classification according to the Enzyme Commission).
  • the enzymatic hydrolysis reaction is carried out according to an enzyme / substrate ratio (E / S) of between 1/10 and 1/1000.
  • the method comprises, prior to the enzymatic hydrolysis, a blood dilution step, so as to obtain a solution which contains between 1 and 12% by weight of hemoglobin.
  • this dilution is carried out using water.
  • the pH adjustments to acid values are carried out using hydrochloric acid, phosphoric acid or sulfuric acid mixture.
  • the adjustment of the pH to a basic value is, for its part, carried out using hydroxide or sodium carbonate, calcium hydroxide, ammonium hydroxide or a mixture of said compounds.
  • the method is carried out on blood rich in nucleic acids such as poultry blood and comprises, after stopping the hydrolysis reaction and before the bleaching of the hydrolysis product, a step of separating the nucleic acids from the remainder of the hydrolysis product and recovering this fraction.
  • the separation of the nucleic acids from the rest of the product of the hydrolysis is carried out by a physical separation method of the type known to those skilled in the art, for example by centrifugation.
  • the fraction obtained at the end of the process contains more than 93% of nucleic acids.
  • the invention also relates to a peptide hydrolyzate such as that obtained from the process described above.
  • a peptide hydrolyzate has the following characteristics:
  • the molecular profile is standardized and the composition of the peptides is constant.
  • peptides with opioid, antihypertensive, analgesic, bradykinin potentiating, hematopoietic, hypolipidemic or coronary-constricting activities are identified.
  • hydrolyzate is produced from whole blood, peptides derived from plasma proteins are advantageously obtained.
  • the invention also relates to the use of a peptide hydrolyzate obtained by means of a process according to the invention as a natural antimicrobial agent and / or an antioxidant, in particular as a food preservative such as that meat products, in particular intended for animals, as a nutritional supplement for animals, to strengthen the animal's immune defenses, to fight against stress and / or to improve the calm and well-being of animals, to regulate the food intake of animals, animals, the animals preferably being pets or livestock, and more preferably dogs or cats.
  • a natural antimicrobial agent and / or an antioxidant in particular as a food preservative such as that meat products, in particular intended for animals, as a nutritional supplement for animals, to strengthen the animal's immune defenses, to fight against stress and / or to improve the calm and well-being of animals, to regulate the food intake of animals, animals, the animals preferably being pets or livestock, and more preferably dogs or cats.
  • the invention also relates to a nucleic acid fraction obtainable by a method as defined above, from poultry blood, the fraction comprising at least 93% of nucleic acids, by weight.
  • the starting material is a mixture of whole blood 70% bovine 30% porcine, recovered from slaughterhouse. To this blood is added sodium citrate (concentration 10% by mass) as anticoagulant from the harvest in slaughterhouse to maintain a homogeneous medium and without loss of raw material. The blood is then introduced into a reactor. The whole is kept at 4 ° C. This step makes it possible to inhibit the growth of contaminants such as bacteria.
  • the hemoglobin concentration is determined and then adjusted to 10% by adding water on the day of the implementation of the process.
  • the solution is brought to ambient temperature (23 ° C.) and the pH is adjusted to 4 by the addition of phosphoric acid diluted to 1 ⁇ 4 volume.
  • phosphoric acid diluted to 1 ⁇ 4 volume.
  • 44000 AU of pepsin per g of hemoglobin are diluted in 0.2 M phosphate buffer at pH 3 and then added to 1 liter of the 70% bovine blood mixture. 30% pig, diluted to 10% hemoglobin.
  • the pH of the reactor is lowered to a value of 3 by adding phosph-volumic phosphoric acid without precipitation of the heme and in a homogeneous medium.
  • the mixture is stirred for 24 hours at 23 ° C.
  • Stopping the hydrolysis is carried out by adding a solution of 30% NaOH to a pH of 9 in the same reactor.
  • the peptide hydrolyzate obtained is homogeneous.
  • Discoloration of the product of the hydrolysis is then carried out by lowering the pH to 4 by adding or-volumic phosphoric acid.
  • the separation of the heme is carried out by centrifugation for 10 minutes at 5000 g.
  • the supernatant containing the recovered peptide hydrolyzate is decolorized. 100% of Theme is recovered in the pellet.
  • the supernatant is dried by lyophilization or atomization.
  • the peptide hydrolyzate obtained was analyzed by mass spectrometry so as to verify and validate the presence of peptides derived from hemoglobin and whose biological activities have been characterized.
  • Bibliographic references describing the known biological activities of each of these peptides are shown in Tables 1 to 8 below.
  • the starting material is poultry blood, recovered in slaughterhouse. It is immediately added at a level of 10% by weight of a solution of sodium citrate at 10% (weight / volume) as anticoagulant. The blood is then introduced into a reactor. The blood is kept at 4 ° C. with stirring.
  • the blood is diluted to a hemoglobin concentration of 10% (w / v) in the enzyme reactor.
  • the solution is brought to ambient temperature (23 ° C.) and the pH is adjusted to 3 by addition of dilute phosphoric acid (2M).
  • the enzyme a porcine pepsin, dissolved beforehand in a buffer of phosphoric acid and sodium hydrogen phosphate (0.1 M) at pH 3, is introduced into the reactor at an enzyme / substrate ratio of 1: 1. 50 (mole / mole).
  • the total duration of the hydrolysis is 24 hours from the introduction of the enzyme. It is carried out with constant stirring and thermostat.
  • the decolorization of the peptide hydrolyzate is carried out by lowering the pH to a value of 4 by adding dilute phosphoric acid (2 M).
  • Separation of the discolored hydrolyzate and the heme fraction is carried out by centrifugation (4000 g, 15 min).
  • the supernatant contains the discolored peptide hydrolyzate, that is to say without heme (at least 99% of peptides (weight)).
  • the pellet represents the fraction enriched in heme (at least 99% heme (weight)).
  • Adje E. Y., Balti, R., Kouach, M., Dhulster, P., Guillochon, D. & Nedjar-Arroume,
  • Barkhudaryan N.A., Oberthuer, W., Lottspeich, F. & Galoyan, A. (1992). "Structure of hypothalamic coronary-constrictory peptide factors”. Neurochemical Research, 17, 1217-1221.

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  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Polymers & Plastics (AREA)
  • Zoology (AREA)
  • Food Science & Technology (AREA)
  • Health & Medical Sciences (AREA)
  • Animal Husbandry (AREA)
  • Biochemistry (AREA)
  • Wood Science & Technology (AREA)
  • Microbiology (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Organic Chemistry (AREA)
  • General Chemical & Material Sciences (AREA)
  • Biotechnology (AREA)
  • Molecular Biology (AREA)
  • Physiology (AREA)
  • Biomedical Technology (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Birds (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • General Engineering & Computer Science (AREA)
  • General Health & Medical Sciences (AREA)
  • Genetics & Genomics (AREA)
  • Nutrition Science (AREA)
  • Peptides Or Proteins (AREA)
  • Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)
EP19716444.5A 2018-04-17 2019-04-15 Verfahren zur gewinnung eines peptidhydrolysats aus tierischen blutproteinen und auf diese weise gewonnenes peptidhydrolysat Pending EP3780967A1 (de)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
FR1853361A FR3080115B1 (fr) 2018-04-17 2018-04-17 Procede d'obtention d'un hydrolysat peptidique a partir de proteines de sang d'animaux, et hydrolysat peptidique ainsi obtenu
PCT/EP2019/059614 WO2019201830A1 (fr) 2018-04-17 2019-04-15 Procede d'obtention d'un hydrolysat peptidique a partir de proteines de sang d'animaux, et hydrolysat peptidique ainsi obtenu

Publications (1)

Publication Number Publication Date
EP3780967A1 true EP3780967A1 (de) 2021-02-24

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EP19716444.5A Pending EP3780967A1 (de) 2018-04-17 2019-04-15 Verfahren zur gewinnung eines peptidhydrolysats aus tierischen blutproteinen und auf diese weise gewonnenes peptidhydrolysat

Country Status (3)

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EP (1) EP3780967A1 (de)
FR (1) FR3080115B1 (de)
WO (1) WO2019201830A1 (de)

Families Citing this family (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN110904177B (zh) * 2019-11-28 2021-10-22 湖北瑞邦生物科技有限公司 一种猪血球多肽粉及其制备方法与应用
EP4213639A1 (de) * 2020-09-17 2023-07-26 Universidade Católica Portuguesa - UCP Neue hydrolysate zur bekämpfung von infektionen sowie verfahren dafür und verwendungen davon
CN112481342A (zh) * 2020-12-11 2021-03-12 湖北省农业科学院农产品加工与核农技术研究所 一种同步制备禽血血红素与抗氧化血肽的方法
CN115386000B (zh) * 2022-09-14 2024-12-03 江苏省农业科学院 一种禽血球加工副产物制备脱色肽和血红素肽的方法

Family Cites Families (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE2831338C2 (de) * 1978-07-17 1985-03-14 Nordfleisch Ag, 2000 Hamburg Verfahren zur Herstellung eines weitgehend hämfreien, partiell hydrolysierten Blut-Eiweißprodukts und Blut-Eiweißprodukt
FR2561074B1 (fr) 1984-03-15 1986-10-31 Lille I Universite Sciences Te Procede de decoloration de substances colorees par des composes tetrapyrroliques, et produits obtenus
FR2635114A1 (fr) * 1988-08-02 1990-02-09 Cibevial Sa Procede de traitement de solutions proteiques contenant des pigments tels que groupements heminiques ou chlorophylles en vue de leur decoloration et produits obtenus
FR2724173B1 (fr) * 1994-09-02 1996-11-15 Eleveurs De La Champagne Sa Procede pour obtenir des produits actifs riches en adn
CN1053195C (zh) * 1997-08-04 2000-06-07 李京华 从鸡血中提取鸡核酸及核蛋白的方法
FR2855722B1 (fr) * 2003-06-04 2005-07-15 Cie Generale De Dietetique Procede biologique d'obtention d'une preparation alimentaire a base de fer hemique ainsi que preparation alimentaire obtenue suite a la mise en oeuvre de ce procede

Also Published As

Publication number Publication date
WO2019201830A1 (fr) 2019-10-24
FR3080115A1 (fr) 2019-10-18
FR3080115B1 (fr) 2022-04-08

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