WO1990001023A1 - Procede de solubilisation de materiaux keratiniques au moyen d'une solution alcaline de peroxyde d'hydrogene - Google Patents

Procede de solubilisation de materiaux keratiniques au moyen d'une solution alcaline de peroxyde d'hydrogene Download PDF

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Publication number
WO1990001023A1
WO1990001023A1 PCT/US1989/003100 US8903100W WO9001023A1 WO 1990001023 A1 WO1990001023 A1 WO 1990001023A1 US 8903100 W US8903100 W US 8903100W WO 9001023 A1 WO9001023 A1 WO 9001023A1
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Prior art keywords
keratin
solution
alkaline
protein
keratinaceous
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PCT/US1989/003100
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English (en)
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Glenn H. Kawasaki
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American Biogenetics Corporation
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Publication of WO1990001023A1 publication Critical patent/WO1990001023A1/fr

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    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
    • A61K47/02—Inorganic compounds
    • 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
    • A23J3/30—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
    • A23K10/00—Animal feeding-stuffs
    • A23K10/20—Animal feeding-stuffs from material of animal origin
    • A23K10/26—Animal feeding-stuffs from material of animal origin from waste material, e.g. feathers, bones or skin
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K33/00—Medicinal preparations containing inorganic active ingredients
    • A61K33/40—Peroxides
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K9/00—Medicinal preparations characterised by special physical form
    • A61K9/0012—Galenical forms characterised by the site of application
    • A61K9/0014—Skin, i.e. galenical aspects of topical compositions
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07C—ACYCLIC OR CARBOCYCLIC COMPOUNDS
    • C07C227/00—Preparation of compounds containing amino and carboxyl groups bound to the same carbon skeleton
    • C07C227/28—Preparation of compounds containing amino and carboxyl groups bound to the same carbon skeleton from natural products
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
    • A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs

Definitions

  • the present invention relates to a chemical process for degrading keratinaceous materials.
  • Keratin is a fibrous protein which is characteristic of the skin or integument of animals and all the specialized derivatives of that integument: the hair, fur, hoofs, and nails of mammals, and the feathers and beaks of birds. These body tissues require high tensile strength to serve their purpose; moreover they must be resistant to solubilization, either aqueous, chemical or enzymatic. Keratin provides strength and structural stability to such tissues primarily because.it has a high concentration of the amino acid cysteine. Cysteine molecules are able to combine with each other through stable disulfide bridges and in so doing link together different polypeptides or different parts of the protein molecule.
  • keratin is cysteine-rich it is extensively cross-linked, tightly packed and dense. The effect is enhanced by the small size of its other major amino acids, glycine and ⁇ erine. Keratin is largely indigestible because its tight packing makes the peptide bonds of its constituent amino acids physically inaccessible to proteolytic enzymes of the digestive tract. For this reason it is not a useful food source; and keratinaceous materials, comprising a significant proportion of an animal's total protein, are often discarded or diverted to non-food uses by the meat processing industry. r The protein in these animal by-products could be made available by treatment of keratin to break its disulfide bonds and convert it to a soluble state in which peptide bonds are exposed. Chemical methods to solubilize keratin include various oxidative or reductive treatments.
  • Ma suda (U.S. Patent No. 4,141,888) used urea or thiourea to solubilize feathers, fur, hair and hoofs. Kikkawa
  • Kadri U.S. Patent No. 4,172,073 describes the use of high pressure steam to solubilize keratinaceous materials.
  • this non-chemical method requires expensive equipment and is inherently dangerous to workers.
  • Solubilized keratin is a source of amino acids and is particularly rich in cysteine, which may be conveniently isolated from the other amino acids by conventional methods. Cysteine can then be converted into derivatives which have added value.
  • Certain skin disorders involve processes of hyperkeratinization which produce unsightly lesions.
  • Keratinase enzymes have been used for this purpose, but they are expensive and, because of their protein nature, have the capacity to raise an immune response in the patients.
  • keratinaceous materials may be solubilized by treating them with hydrogen peroxide in an alkaline aqueous solution under conditions of ordinary temperature and pressure.
  • the treatment does not involve hazardous materials or leave toxic or unpalatable residues in foodstuff.
  • the principal reagent, hydrogen peroxide can be produced cheaply from alcohol by an enzymatic process that we have developed that utilizes alcohol oxidase from Hansenula polvmorpha.
  • a method for hydrolyzing keratinaceous materials comprising contacting the keratinaceous material with an alkaline solution which contains hydrogen peroxide.
  • the alkaline solution is that of a hydroxide compound, such as NaOH, KOH or NH 4 0H at a concentration sufficient to produce an initial pH of at least 9.
  • the alkaline solution has a pH of at least 11.
  • the method further comprises the acid hydrolysis of peptides to amino acids.
  • the acid hydrolysis of the peptides is carried out by means of a hydrochloric acid digestion.
  • the method further comprises the isolation of specific amino acids from the acid hydrolysis product.
  • the keratinaceous material is obtained from a vertebrate species, and in a preferred embodiment the material is obtained from avian or mammalian species.
  • the keratinaceous material is feathers and down.
  • the keratinaceous source material is wool' or hair, and in yet other embodiments the keratinaceous material may be hides or skins of animals.
  • the keratinaceous material may comprise fish skin or scales.
  • hydrolyzed protein which is produced by treating keratinaceous materials with alkaline hydrogen peroxide.
  • the hydrolyzed protein produced comprises a mixture of polypeptides, oligopeptides and peptides which'is usable as a feed supplement for amino acids.
  • a hydrolyzed protein which is derived from the feathers and down of birds.
  • the invention further provides amino acids mixtures produced from the solubilization of keratinaceous material, followed by hydrolysis -of protein and peptides to amino acids.
  • the hydrolysis of the proteins and peptides may be carried out by treatment with acid, preferably hydrochloric acid, treatment with base, or digestion with proteolytic enzymes.
  • the hydrolysis may also be carried out by continued treatment with an alkaline solution of hydrogen peroxide.
  • this amino acid mixture is derived from the protein of the feathers and down of birds or from fish meal.
  • a method for solubilizing keratin by means of treatment with hot alkaline solution preferably at a temperature of at least about 100*C.
  • a method for hydrolyzing keratin in a zone in the skin of an animal which comprises contacting the zone of the skin with an alkaline solution of hydrogen peroxide and then allowing the solution to remain in contact with the zone of the skin until the amount of keratin is substantially reduced or degraded.
  • the method is used to facilitate transder al delivery of a therapeutic agent by hydrolyzing and solubilizing the keratin of skin to reduce the normal resistance of the zone of the skin to fluid penetration.
  • the method is used in treating a dermatological disorder of hyperkeratinization by removing the keratin from a zone on skin by the method of alkaline hydrogen peroxide treatment described.
  • a medicament for topical use which comprises effective concentration of hydrogen peroxide together with an alkaline agent in an inert base.
  • the alkaline hydrogen peroxide method may be used to solubilize keratinaceous material which has accumulated in drain lines and filters and which blocks the flow therethrough.
  • Alkaline solutions of hydrogen peroxide (H2O2) are capable of solubilizing keratinaceous materials so as to make the endogenous protein available as a food supplement, and as the source of other commercially valuable protein products.
  • Keratinaceous materials which can be usefully treated comprise the feat ers of wild and domestic fowl, including chickens, turkeys, ducks and geese, the hoofs, hides, horns, beaks, claws, scales, nails, skin, hair and wool and the membranes of egg shells. Much of this protein-rich material is now discarded as waste. Other salvageable keratinaceous material is found in discarded animal parts and eggs containing unborn chicks.
  • the present invention is described in terms of chicken feathers, an important waste by-product of the food industry, but it is understood the method is generally applicable to similar materials.
  • An alkaline solution containing as little as 1% H 2 O 2 is effective in solubilizing common keratinaceous materials at ordinary room temperatures.
  • the solution may be made alkaline by the addition of any basic substance, but preferably the base is a hydroxide of a monovalent cation, for example IT 1" , Na + or NH_j + , whose neutralization products are relatively soluble and are harmless in food products.
  • the efficiency of the process is affected by pH, the presence of metal cations, and the ratio of solution to the keratin source. Solubilization of keratinaceous material is poor in hydrogen peroxide solutions where the pH is less than 9; however, when a solution of 1% H2O 2 is brought to pH 10 by adding roughly 1* by weight of NaOH it can release over 80% of the weight of crude keratin chicken feathers as soluble protein (Example 3) .
  • Example 2 The presence of low concentrations of divalent metal ions in those solutions of Example 3 containing FeS ⁇ 4 and nCl2 apparently reduced the yield of protein solubilized from the keratin of feathers, presumably by decomposing H 2 O2 under the alkaline conditions. The weight ratio 5:1 for feathers:peroxide remained optimum for 2-fold differences in the weights of each. (Example 2)
  • the present invention is superior to other keratin solubilization procedures in terms of costs, convenience and safety.
  • the alkaline peroxide method can be carried out at room temperature without using special equipment. It is ⁇ superior to known chemical methods, such as hydrolysis with dimethylformamide (Goodwin U.S. Patent No. 3,970,614) which requires boiling under reflux with high concentrations of expensive solvent from which the protein product must then be extracted and separated by precipitation. It is also preferable to reducing hydrolysis which must be carried out in an atmosphere of inert gas. (Kadri U.S. Patent No. 4,172,073).
  • the reagents used in alkaline peroxide solubilization are inherently safe when used at the low concentrations required.
  • Hydrogen peroxide (which remains in the reaction mixture) decomposes to harmless oxygen and water.
  • the NaOH remaining can be diluted out to reduce the pH of the reaction mix to neutrality or can be neutralized with HC1 or acetic acid to harmless soluble salts.
  • Alkaline peroxide solubilization of keratinaceous material converts biological waste into available protein more efficiently than alternative processes.
  • Protein from solubilized keratin is important also as a source of peptides and amino acids.
  • the protein may be further broken down, to peptides and/or amino acids by known methods of proteolysis.
  • the principal methods are acid or base hydrolysis and enzymatic digestion.
  • Acid or base act non- selectively on peptide bonds to convert protein to its constituent amino acids.
  • the proteolytic enzymes act selectively on a few of peptide bonds to convert proteins to peptides or oligopeptides, containing from a few to a substantial number of amino acids.
  • the number and size of hydrolyzed peptides an enzyme produces is related to the enzyme's specificity.
  • trypsin has a specificity for peptide bonds involving lysine or arginine, and two less common acid cuids, so trypsin digestion produces a small number of relatively large peptides; by comparison pepsin hydrolyses peptide bonds involving six of the more common amino acids, and pepsin digestion produces a large number of relatively small peptide.
  • solubilized keratin can be further hydrolyzed to any chosen extent by selecting the hydrolyzing agent appropriately.
  • hydrolyzed protein products may be used for a vari-ety of commercial purposes, non-nutritive as well as nutritive.
  • nutritive use the entire protein product from solubilized keratin may be added to a food product to improve its protein content.
  • selected amino acids usually the essential amino acids.are isolated from protein hydrolysales derived from solubilized keratin and added to food products as * supplements. Also, individual amino acids may be thus isolated for use as food supplements.
  • the supplemented foods may be used in either animal or human nutrition.
  • cysteine in keratin makes its protein hydrolysates suitable for dietary supplements requiring this amino acid or related derivatives.
  • Pet cats which have been fed some commercial cat foods may develop a degenerative disease of the myocardium leading ultimately to heart failure. This disorder can be reversed by feeding cats a diet supplemented in taurine.
  • Taurine is the decarboxylation product of cysteic acid, and conversion of the cysteine to taurine via decarboxylation may provide a food supplement for cats which supplies an abundant supply of taurine (Example 6).
  • the method of the present invention is a safe and effective means to solubilize skin keratin in situ in living animals, including humans, and consequently can be applied in various therapies.
  • the keratin solubilization can be used as an adjunct therapy in ameliorating the discomforts of certain der atological diseases.
  • Non ⁇ inflammatory epidermal hyperplasia marked by a keratinaceous excrescence of skin or thickened stratum corneum without neovascularization are particularly appropriate for this type of treatment.
  • the method can also be used to increase the trans- dermal drug delivery provided by drug-impregnated skin patches.
  • Pre-treat ent of the zone of skin to which the patch is to be applied will solubilize the keratin in the upper layers of the epidermis, allowing it to be dissolved away, and the dekeratinized skin will then offer less resistance to the uptake of the drug.
  • the degree and rate of dekeratinization of the skin area can be controlled by factors such as the vehicle in which the H2O 2 is applied, the concentration of H 2 O 2 and the buffering pH.
  • the preferred substrate for experimental dermal treatments is skin from the Yucatan hairless micro-pig (HMP) (Lavker, R.M., et al. 1988. J. Invest. Dermatol. 90:580) as described in Example 8.
  • HMP Yucatan hairless micro-pig
  • skin from other pigs or various rodents especially "nude” varieties
  • rodents especially "nude” varieties
  • the alkaline peroxide formulations may be combined with suitable carriers, such as aqueous propylene glycol mixtures,in the patch and applied to the skin surface for varying lengths of time.
  • the patch may comprise an occlusion chamber with gauze or other absorbent material to hold differing amounts of the alkaline peroxide formulation.
  • the formulation may include detergents, solvents, soaps, and/or abrasives.
  • a preferred treatment time is 48 hours or less. A more preferred treatment time is less than two hours. Patches for the longer time points are placed on the animal earlier, so that all time points may be assayed together.
  • Alkaline peroxide treatments may also remove keratinaceous layers of the stratum corneum to reduce wrinkles.
  • alkaline peroxide may substitute in part for drugs, such as retinoid acid (Retin-A; for a mini-review see Roberts, L. 1988. Science 239:564) and other vitamin A derivatives which interfere with the synthesis of skin keratins and thereby reduce the level of wrinkles.
  • Alkaline peroxide treatment may also reduce cross-linking of non-keratinaceous substances, such as collagen or lipoproteins, to increase the flexibility of the skin. The ability of alkaline peroxide treatment to solubilize the keratin in the hair shaft can be exploited in various applications.
  • the method can also be used cosmetically in depilation or removal of hair from skin by allowing the 5 process to proceed until the hair shaft is destroyed. More vigorous depilation conditions, optionally accompanied by mechanical scrubbing or abrasion can adapt the method to the removal of hair from animal hides.
  • the solubilization method further has obvious uses in XO destroying hair or other keratinaceous material that forms an obstruction in any mechanical orifice, whether in bulk as a plug in plumbing drains, or as fine particles of hair which reduce the efficiency of combing, shearing or shaving instruments.
  • Flasks 1, 2, and 3 were placed on gyrator shakers (140 RPM) at ambient room temperature for three days. Flasks 4 and 5 were autoclaved at 15 psi, 120* C. for 20 minutes. Substantial solubilization of the feathers was visually noticeable in flask 3 after the
  • a quantity of 400 mg of avian feather clippings were placed in each of several flasks containing a volume of 20 ml of 1% H 2 O 2 .
  • the solutions in these sets of flasks were adjusted to acidic, neutral, and alkaline pH respectively, and Fe +2 and Mn +2 compounds added to sets of solution ' s at the various pH levels as indicated in the table.
  • the feathers were treated in these solutions for 3 days, at which time the soluble protein concentration was
  • EXAMPLE 4 Amino Acid Analysis of Alkaline , Peroxide-Treated Feathers
  • the solubilized proteins from flasks 3 and 4 in Example 1 were acid-hydrolyzed with hydrochloride vapors in sealed, air-evacuated glass tubes at 110* C. for 24 hours.
  • Amino acid determinations for this hydrolysate were carried out by the PTC method on a Hewlett Packard 1091A HPLC. Absorbances were read at 269 nm, and the data were analyzed (integrated) by a Nelson Data System computer program. Sample peak areas generated by HPLC were converted to amino acid concentrations using concentration/area ratios of known standards.
  • EXAMPLE 5 Solubilizing Wool and Other Hair Undyed wool yarn was cut into lengths of * approximately one inch and weighed into 1.0 gram portions. 5 Each gram was placed into a separate 250-ml Erlenmeyer flask and subjected to a treatment regimen a ⁇ in Example One, except that the room temperature reactions were terminated after two days by placing the flasks into a 4*C. coldbox. 0 The unfiltered liquid content of each flask was measured for soluble protein by the method of Lowxy with BSA as standards. The following table gives the total amount of protein that was solubilized from one gram of wool by each treatment. 5 Water Only 1.4 mg
  • Cysteine accounts for approximately 8% of feather amino acids by weight.
  • cysteine is not directly quantifiable by the PTC methods.
  • the sample may be treated with performic acid to oxidize cysteine to cysteic acid, which may then be measured by the PTC method.
  • the total amount of sulfur-containing amino acids in the protein product is an important parameter for use of the solubilized keratin as a food supplement.
  • cysteic acid is an intermediate in the formation of taurine from cysteine and may be a dietary substitute for taurine, since taurine may be generated from cysteic acid by decarboxylation.
  • Performic acid was generated by mixing 450 ul of 30% H 2 0 2 with 50 ul of 88% formic acid at -10*C. and incubating this reaction at -10"C for 2 hr in a saltwater- ice bath. 12.5 ul of the neutralized product (100 ug of protein) was added to the 500 ul of performate and held at -10*C. As a control, 12.5 ul of product was incubated with 500 ul of distilled water at the same temperature. After two hours, 2 ml of distilled water was added to each sample and the samples were frozen at -20*C. Both samples were lyophilized and analyzed for amino acid composition as previously described. The following tables summarize the amino acid composition of 1) performate-treated product and 2) untreated product.
  • cysteic acid levels are approximately 7% of the solubilized keratin. This observation indicates that nearly all of the cysteine had been converted to cysteic acid by the alkaline peroxide treatment. However, the secondary performate regimen slightly to increase the amount of cysteic acid in the solubilized keratin. Performate treatment appears to stabilize certain amino acids. The total amount of sulfur-containing amino acids was found to be 8.9% by weight in this study of solubilized feathers.
  • Epidermis of the Yucatan hairless micro-pig is treated with 0 to 50% hydrogen peroxide in 0 to 5% sodium hydroxide solution for time points up to 48 hours.
  • the treated skins are tested for permeability at 35-37"C. in Franz diffusion chambers (Franz, T.J. 1978. Curr. Prob. Der atol. 7:58-68) or other two-chambered apparati with isotope-labelled drugs, such as 14 C-diazepam or 3 H- hydrocortisone , or other compounds as diagnostic markers of diffusion across the membranes.
  • Skin biopsies (about 4mm) are taken, and sections are made to examine histological changes in the stratum corneum.
  • treated animals are sacrificed; and the skins are tested for permeability in the diffusion chambers noted above.
  • HMP skins were treated with 15% hydrogen peroxide in 4% sodium hydroxide solution for 30 minutes. Water was used as a control on other skins. Alkaline peroxide treated skin showed 4 times the permeability of hydrocortisone compared to the control skin in a time course of 24 hours.

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Abstract

On peut solubiliser des plumes, des poils, de la laine et d'autres matériaux essentiellement composés de kératine dans des solutions alcalines qui contiennent du peroxyde d'hydrogène en faible concentration. La solubilisation est pratiquement totale à des températures ambiantes et sous des pressions atmosphériques normales, ce qui permet de transformer plus de 75 % en poids de la source de kératine en produits peptidiques. Ces peptides ou mélanges d'acides aminés obtenus par hydrolyse des peptides sont riches en dérivés de cystéine et sont utiles comme compléments alimentaires à ajouter au fourrage d'animaux. Le procédé de solubilisation proprement dit peut avoir des applications thérapeutiques en médecine humaine et vétérinaire.
PCT/US1989/003100 1988-07-19 1989-07-18 Procede de solubilisation de materiaux keratiniques au moyen d'une solution alcaline de peroxyde d'hydrogene WO1990001023A1 (fr)

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Cited By (15)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5276138A (en) * 1990-09-17 1994-01-04 Kurashiki Boseki Kabushiki Kaisha Process for solubilizing animal hair
WO1994014169A1 (fr) * 1992-12-09 1994-06-23 Waste Reduction By Waste Reduction, Inc. Procede et appareil de destruction de cadavres d'animaux radiomarques
US5376042A (en) * 1991-06-19 1994-12-27 Peroxidos Do Brasil Ltd. Process for the depilation of animal skins
WO1998053847A1 (fr) * 1997-05-29 1998-12-03 Ben Gurion University Of The Negev Research And Development Authority Systeme de transport transdermique
US5981204A (en) * 1997-05-06 1999-11-09 Johnson; Ted Donald Method for forensically screening hair samples for the presence of cannabinoids
US6667052B2 (en) 1997-05-29 2003-12-23 Ben Gurion University Of The Negev Research And Development Authority Transdermal delivery system
WO2005002354A1 (fr) 2003-06-24 2005-01-13 Cargill, Incorporated Recuperation de peptones
WO2006105958A1 (fr) * 2005-04-06 2006-10-12 Vomm Chemipharma S.R.L. Procede et usine pour la production de farines animales dont la biodisponibilite des acides amines est amelioree
US7297354B2 (en) 2000-04-26 2007-11-20 Land O'lakes, Inc. Protein material
WO2014013081A2 (fr) * 2012-07-20 2014-01-23 Dupont Nutrition Biosciences Aps Procédé
EP2832236A1 (fr) * 2013-07-30 2015-02-04 Tessenderlo Chemie NV Procédé de production de matériau contenant de la kératine hydrolysée
KR101537348B1 (ko) * 2014-08-26 2015-07-16 (주)우리비앤비 도축 부산물의 처리방법
WO2015014860A3 (fr) * 2013-07-30 2015-08-06 Tessenderlo Chemie N.V. Procédé de production d'une substance kératinique hydrolysée
WO2015138848A1 (fr) * 2014-03-14 2015-09-17 Peroxychem, Llc Traitement d'eau et de sol contaminés
ES2801025A1 (es) * 2019-06-26 2021-01-07 Univ Navarra Publica Metodo de obtencion de queratinas y bioplasticos a partir de residuos queratinosos de animales

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US3464825A (en) * 1967-02-28 1969-09-02 Gen Mills Inc Keratin protein product and process of preparing same
US4088596A (en) * 1976-02-27 1978-05-09 Kao Soap Co., Ltd. Method of treating drains
US4438102A (en) * 1982-08-10 1984-03-20 Ciro's Touch, Ltd. Method of promoting tissue growth
JPS6168426A (ja) * 1984-09-12 1986-04-08 Fuji Oil Co Ltd 低フエニルアラニンペプチド混合物の製造法
US4664836A (en) * 1985-09-18 1987-05-12 Amway Corporation Drain cleaner
US4705682A (en) * 1985-05-13 1987-11-10 Henkel Kommanditgesellschaft Auf Aktien Oligopeptide derivatives, their production and their use as surfactants gentle to the skin

Patent Citations (8)

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Publication number Priority date Publication date Assignee Title
US2158499A (en) * 1939-05-16 Method for decomposing scleropro
US2719813A (en) * 1953-09-10 1955-10-04 Procter & Gamble Reducing hair waving lotion
US3464825A (en) * 1967-02-28 1969-09-02 Gen Mills Inc Keratin protein product and process of preparing same
US4088596A (en) * 1976-02-27 1978-05-09 Kao Soap Co., Ltd. Method of treating drains
US4438102A (en) * 1982-08-10 1984-03-20 Ciro's Touch, Ltd. Method of promoting tissue growth
JPS6168426A (ja) * 1984-09-12 1986-04-08 Fuji Oil Co Ltd 低フエニルアラニンペプチド混合物の製造法
US4705682A (en) * 1985-05-13 1987-11-10 Henkel Kommanditgesellschaft Auf Aktien Oligopeptide derivatives, their production and their use as surfactants gentle to the skin
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US5376042A (en) * 1991-06-19 1994-12-27 Peroxidos Do Brasil Ltd. Process for the depilation of animal skins
WO1994014169A1 (fr) * 1992-12-09 1994-06-23 Waste Reduction By Waste Reduction, Inc. Procede et appareil de destruction de cadavres d'animaux radiomarques
US5981204A (en) * 1997-05-06 1999-11-09 Johnson; Ted Donald Method for forensically screening hair samples for the presence of cannabinoids
WO1998053847A1 (fr) * 1997-05-29 1998-12-03 Ben Gurion University Of The Negev Research And Development Authority Systeme de transport transdermique
US6274166B1 (en) * 1997-05-29 2001-08-14 Ben Gurion University Of The Negev Research And Development Authority Transdermal delivery system
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US7297354B2 (en) 2000-04-26 2007-11-20 Land O'lakes, Inc. Protein material
WO2005002354A1 (fr) 2003-06-24 2005-01-13 Cargill, Incorporated Recuperation de peptones
WO2006105958A1 (fr) * 2005-04-06 2006-10-12 Vomm Chemipharma S.R.L. Procede et usine pour la production de farines animales dont la biodisponibilite des acides amines est amelioree
WO2014013081A2 (fr) * 2012-07-20 2014-01-23 Dupont Nutrition Biosciences Aps Procédé
WO2014013081A3 (fr) * 2012-07-20 2014-04-10 Dupont Nutrition Biosciences Aps Procédé
EP2832236A1 (fr) * 2013-07-30 2015-02-04 Tessenderlo Chemie NV Procédé de production de matériau contenant de la kératine hydrolysée
WO2015014860A3 (fr) * 2013-07-30 2015-08-06 Tessenderlo Chemie N.V. Procédé de production d'une substance kératinique hydrolysée
CN105517449A (zh) * 2013-07-30 2016-04-20 泰森德洛化学公司 用于制备水解的角蛋白材料的方法
US10154678B2 (en) 2013-07-30 2018-12-18 Tessenderlo Chemie N.V. Method for producing hydrolysed keratinaceous material
CN105517449B (zh) * 2013-07-30 2020-02-14 泰森德洛集团公司 用于制备水解的角蛋白材料的方法
EP3027066B1 (fr) 2013-07-30 2021-07-14 Tessenderlo Group NV Procédé de production d'une substance kératinique hydrolysée
WO2015138848A1 (fr) * 2014-03-14 2015-09-17 Peroxychem, Llc Traitement d'eau et de sol contaminés
KR101537348B1 (ko) * 2014-08-26 2015-07-16 (주)우리비앤비 도축 부산물의 처리방법
ES2801025A1 (es) * 2019-06-26 2021-01-07 Univ Navarra Publica Metodo de obtencion de queratinas y bioplasticos a partir de residuos queratinosos de animales

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