Classifications

• • C—CHEMISTRY; METALLURGY
  • C07—ORGANIC CHEMISTRY
  • C07K—PEPTIDES
  • C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
  • C07K1/12—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by hydrolysis, i.e. solvolysis in general
  • C07K1/122—Hydrolysis with acids different from HF
• • 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
  • 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
  • A23J1/006—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from vegetable 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
  • 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
  • A23J3/14—Vegetable 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
• • C—CHEMISTRY; METALLURGY
  • C07—ORGANIC CHEMISTRY
  • C07K—PEPTIDES
  • C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
  • C07K1/14—Extraction; Separation; Purification
  • C07K1/34—Extraction; Separation; Purification by filtration, ultrafiltration or reverse osmosis
• • C—CHEMISTRY; METALLURGY
  • C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
  • C08L—COMPOSITIONS OF MACROMOLECULAR COMPOUNDS
  • C08L89/00—Compositions of proteins; Compositions of derivatives thereof
  • C08L89/04—Products derived from waste materials, e.g. horn, hoof or hair

Definitions

• the present invention relates to a method for producing a protein hydrolyzate.
• the present invention relates to a method for producing a keratin hydrolyzate.
• Protein hydrolysates are used today as raw materials in a wide variety of industrial sectors due to their wide range of applications and their generally good availability.
• An exemplary field of application is the production of cosmetic articles or personal care products.
• As a source of raw material for the production of protein hydrolysates vegetable or animal substrates are used. It can also be used residual materials, such as those incurred in the processing of such plants or animals in other areas, such as the food industry.
• a protein used to produce hydrolysates only to a very limited extent is keratin, although corresponding sources of keratin are present in large quantities. For example, in the field of poultry farming, large quantities of feathers are produced, which have a very high keratin content.
• keratin a protein used to produce hydrolysates only to a very limited extent
• large quantities of feathers are produced, which have a very high keratin content.
• hydrolysis of proteins of plant origin or collagen-containing proteins of animal origin usually no
• CONFIRMATION COPY Proteins has a high number of disulfide bridges. These disulfide bridges give the keratin its high strength. At the same time, however, they complicate the decomposition of keratin in the hydrolysis. In order to provide the keratin contained in, for example, feathers, wool, or horn for further processing, the protein scaffold must be destroyed.
• the hydrolytic cleavage in aqueous solution is known from the prior art.
• a keratin-containing raw material such as wool is exposed to an elevated temperature (for example, about 150 ° Celsius) and an elevated pressure (for example, about 350 kPa) for a period of 30 to 70 minutes.
• EP-A 0 499 261 describes a method for the hydrolysis of keratin in which a keratin-containing material is first treated with an aqueous solution containing sulfite ions and then converted into keratin hydrolyzate with the aid of a proteolytic enzyme.
• the pretreatment with the solution containing sulfite ions is carried out at a pH of 6 to 9, at a temperature of 60 to 100 ° C for a period of 10 minutes to 4 hours.
• the subsequent proteolysis is carried out by multi-stage entry of the pretreated, keratin-containing material into the enzyme-containing hydrolysis mixture.
• the disadvantage is the described method the fact that no continuous treatment of keratin-containing material is possible.
• the reaction times required in the enzymatic reaction are very long and it is necessary a final thermal deactivation of the enzymes used, to which the solutions must be heated to temperatures of about 90 ° C.
• WO 02/36801 A1 describes a protein hydrolyzate which is obtained by continuous enzymatic hydrolysis of a protein-containing substrate, wherein the hydrolysis described is carried out in an extruder.
• the protein hydrolysates thus prepared show a significantly improved interfacial activity and a negative redox potential.
• improved interfacial activity is to be understood in particular as meaning that the protein hydrolysates prepared according to the invention reduce the interfacial tension to a range which has hitherto been known only from conventional O / W emulsifiers.
• the protein hydrolysates prepared according to the invention thus offer themselves as emulsifiers / dispersants for corresponding industrial applications.
• the complexing agent is selected from the group consisting of ethylenediaminetetraacetic acid (EDTA), nitriloacetic acid (NTA), ethylene glycol bis (aminoethyl ether) -N, N'-tetraacetic acid (EGTA), ethylenediamine disuccinic acid (EDDS), citric acid, 2,3-dihydroxybutanedioic acid, piroctone-olamine, phytochelatins, natural or artificial polypeptides and Amino acids, crown ethers, their derivatives or mixtures of these.
• EDTA ethylenediaminetetraacetic acid
• NTA nitriloacetic acid
• EGTA ethylene glycol bis (aminoethyl ether) -N, N'-tetraacetic acid
• EDDS ethylenediamine disuccinic acid
• citric acid 2,3-dihydroxybutanedioic acid
• piroctone-olamine piroc
• a “protein hydrolyzate” in the sense of the invention is understood as meaning a mixture which consists of at least about 15% by weight of polypeptides or oligopeptides which have been formed by chemical cleavage of the protein to be hydrolyzed.
• the polypeptides or oligopeptides predominantly have a molecular weight which is lower than the molecular weight of the protein before the hydrolysis.
• the protein hydrolysates prepared by the process according to the invention can in principle be prepared from all suitable protein sources. However, protein sources which contain at least keratin as protein are preferably used in the method according to the invention. Within the scope of a preferred embodiment of the process according to the invention, the protein hydrolysates obtained therefore contain hydrolysis products, as obtainable by the degradation of keratin.
• protein sources containing more than one type of protein are used to prepare the protein hydrolysates according to the invention.
• protein sources which contain collagen or gluten or both in addition to keratin are suitable.
• the protein source for use in the method according to the invention are protein-containing natural products, in particular those obtained from keratin-containing natural products.
• Suitable protein-containing natural products are, for example, natural proteins containing plant proteins, such as corn, wheat, barley, Soy or animal protein products containing substances such as slaughterhouse waste, wool, feathers, hair, hooves, horns, bristles and the like, such as those incurred in the processing of carcasses.
• maritime protein sources such as fish wastes, shellfish wastes and algae can be used as raw materials in the process according to the invention.
• bird feathers, in particular chicken feathers are particularly suitable.
• a keratin-containing substrate such as, for example, horn, hooves, wool or feathers, which is comminuted
• protein source a keratin-containing substrate
• Suitable comminuting methods are, for example, cutting, shredding or grinding.
• feathers when using feathers as a keratin-containing protein source, these are preferably provided in the form of a feather meal.
• Suitable comminution levels for the keratin-containing protein source are, for example, sizes of about 2 cm in the longest extent to some ⁇ .
• springs are used as a keratin-containing protein source, they may for example be pre-shredded such that the quills are broken and the springs have a size of about 1 cm.
• a keratin-containing protein source is preferably provided in the form of a flour having an average particle size of about 10 ⁇ m to 1 mm.
• a protein suspension having a solids content of> 15 wt .-% and ⁇ 70 wt .-%, preferably between> 20 wt .-% and ⁇ 60 wt .-%, more preferably between> 25 wt % and ⁇ 40% by weight. It has been found that a suspension with such a solids content allows good processability with high yield of hydrolyzate.
• Suitable dispersants are, for example, surfactants, such as anionic surfactants, cationic surfactants or nonionic Surfactants.
• suitable anionic surfactants are alcohol sulfates, alcohol ether sulfates and protein surfactants and / or surfactants based on amino acids.
• cationic surfactants are cetyltrimethylammonium bromide (CTAB), cetyltrimethylammonium chloride (CTAC).
• nonionic surfactants are alkoxylates or alkylpolyglucosides.
• hydrolysis result with respect to the molecular weight distribution of the hydrolyzate obtained is independent of the type of surfactant used.
• a protein hydrolyzate obtained from a keratin-containing protein source is used as the surfactant. This reduces the amount of foreign substances within the reaction mixture. Dispersants serve, for example, to increase the reactive surface and to improve the wettability of the protein sources used.
• the surfactant may in a preferred embodiment of the process in the provided protein source suspension in a concentration between 0.1 wt .-% and 50.0 wt .-%, preferably 0.1 wt .-% to 20.0 wt .-% be.
• a base is added which is selected from the group consisting of alkali metal hydroxide, alkaline earth metal hydroxide, calcium oxide, organic bases or mixtures thereof.
• the base is selected from a group consisting of NaOH, KOH, Ca (OH) 2 and CaO. It has surprisingly been found that a sufficient hydrolysis of the protein sources is also possible using these inexpensive and environmentally safe bases.
• the base is added in a ratio of between 1: 3 and 1: 7, based on the solids content in the protein suspension.
• the ratio is to be understood that to a part of base 3 to 7 Parts of solid content can be given in the protein suspension.
• the resulting pH value is in a range> pH 10, preferably between> pH 1 1 and ⁇ pH 14.
• the added complexing agent for example selected from the group consisting of ethylenediaminetetraacetic acid (EDTA), nitriloacetic acid (NTA), ethylene glycol bis (aminoethyl ether) -N, N'-tetraacetic acid (EGTA), ethylenediamine disuccinic acid (EDDS), Citric acid, 2,3-dihydroxybutanedioic acid, phytochelatins, natural or artificial polypeptides and amino acids, crown ethers, their derivatives or mixtures thereof, in the reaction solution in a concentration between 1 * 10 "6 wt .-% and 10 wt .-%, preferably between 1 * 10 "6 wt .-% and 5 wt .-% contained. Such a concentration has proven to be sufficient to substantially prevent the formation of strong-smelling by-products.
• EDTA ethylenediaminetetraacetic acid
• NTA nitriloacetic acid
• EGTA ethylene glyco
• a reducing agent is added to the provided protein source suspension.
• the addition of a reducing agent facilitates the cleavage of the disulfide bridges contained in the keratin-containing proteins.
• inorganic and / or organic reducing agents can be used according to the invention.
• Suitable inorganic reducing agents are, for example, alkali metal dithionite, alkali metal hydrogen sulfite, alkaline earth metal hydrogen sulfite, or mixtures of these.
• Sodium dithionite in particular, has proved to be a preferred reducing agent, since it is low in environmental terms and low in environmental terms as a food-approved substance.
• organic reducing agents are hydrazine, cystine (dimer of cysteine), glutathione disulfide (GSSG), as well as derivatives or mixtures of these.
• the reducing agent can be added in the inventive method in a concentration between 1:20 and 1: 300 based on the solids content in the protein suspension become.
• the ratio is to be understood in such a way that 20 parts of solid in the protein suspension occur for one proportion of reducing agent.
• the resulting mixture of protein suspension, base, complexing agent and optionally reducing agent is heated under elevated pressure, preferably between> HOOmbar and ⁇ 4000mbar, more preferably between 1500mbar and 3000mbar.
• elevated pressure preferably between> HOOmbar and ⁇ 4000mbar, more preferably between 1500mbar and 3000mbar.
• the resulting mixture is heated to a temperature between 100 ° C and 150 ° C, preferably between 110 ° C and 140 ° C. It has been shown that an increase in the pressure and / or an increase in the temperature lead to a significant reduction in the required reaction time.
• reaction time can be increased with an increase in pressure and / or temperature to 1 , 0 to 2.0 hours, preferably 1.5 hours. This results in significant economic and environmental advantages of process management due to the energy saved.
• an acid is added to adjust the pH to a value between> pH 2 and ⁇ pH 8.
• the added acid is selected from the group consisting of halogen acids, in particular hydrochloric or hydrobromic acid, sulfuric acids, phosphoric acids, carboxylic acids, hydroxycarboxylic acids or mixtures thereof.
• sulfuric acids and phosphoric acids are understood to mean corresponding oxidation state variants of the sulfur- or phosphorus-based acids; Halogen acids in this context also include oxidation state variants of the halogen-based acids.
• a filter aid is added to the mixture before the filtration step.
• the term "before the filtration step” is to be understood as meaning that the filter medium can be added both immediately before the filtration step, during the hydrolysis reaction or at the beginning of the reaction mixture.
• Activated carbon can also be added to the reaction solution at the beginning of the process according to the invention
• the filtration step can be carried out using known filter technologies such as filtration via so-called filter bags with different pore openings (from .mu.m to 200 .mu.m)
• centrifuges can be used which transfer the solid constituents of the reaction mixture can separate a filter cloth from the liquid phase.
• the speed of the centrifuge not also the porosity of the filter cloth can be varied for effective separation.
• Such solidification can be carried out, for example, by freeze-drying and / or spray-drying.
• the solid hydrolyzate thus obtained can be transported in an advantageous manner and can be used in a variety of industrial processes due to its water solubility readily.
• a keratin hydrolyzate produced by means of the process according to the invention has a molecular weight distribution between 200 g / mol and 100,000 g / mol, preferably between 4000 g / mol and 5500 g / mol, which is essentially the molecular weight distribution of the prior art corresponds to known keratin hydrolysates obtained, for example, by enzymatic reactions.
• Plantacare 2000 UP (Decyl Glucoside) 4,4562 0,0000 0,0000 0,0000 0,0000 0,0000
• Lamepon S (Potassium Cocoyl 0.0000 0.4617 0.4844 0.0000 0.0000 0.0000 0.0000 Hydrolyzed Collagen)
• the keratin hydrolyzates preparable by the method of the invention have a critical micelle concentration (CMC) in a range from 0.05 mM to 0.5 mM.
• CMC critical micelle concentration
• the CMC of the keratin hydrolyzate prepared by the process according to the invention is significantly lower than the CMC of keratin hydrolysates known from the prior art.
• Such a low CMC contributes to an improved effectiveness of the hydrolyzates prepared according to the invention as detergent or surfactant in washing processes.
• FIG. 1 shows the surface tension of an aqueous solution as a function of Concentration of a keratin hydrolyzate 100 prepared according to the invention and of a comparative product 100 (Kera-Tein, Tri-K Industr.) At a measurement temperature of 25 ° C.
• the critical micelle concentration results from the ordinate value of the inflection point of the respective concentration curve.
• the keratin hydrolyzate prepared according to the invention exhibits a CMC value which is lower by about two orders of magnitude compared to the comparison product. Taking into account an average molecular weight in the range according to the invention thus results in a CMC in a range of about 0.05mM to 0.5mM.
• FIG. 2 shows, by way of example, an IR spectrum of a keratin hydrolyzate 100 produced according to the invention as a dry substance.
• characteristic bands in particular the vibrations at 1035cm “1 and 1120cm " 1 were identified.
• the absorption at 1120 cm -1 is presumably attributable to an NH 2 deformation oscillation (rock) of an aliphatic primary amide, whereas the absorbance at 1035 cm -1 is presumably attributable to a CO stretching vibration of an aliphatic primary alcohol.
• FIG. 3 shows the IR spectrum of a comparison product 200 (Kera-Tein, Tri-K Industr.) In which these characteristic absorption bands are absent.
• FIG. 6 shows a comparison of the ⁇ - ⁇ spectra of a keratin hydrolyzate 100 produced according to the invention and of the comparison product 200 (Kera-Tein). Both spectra show clear differences.
• the comparison product shows a significantly higher number of signals than the hydrolyzate prepared according to the invention, which suggests that the keratin hydrolyzate prepared according to the invention is present as a significantly more uniform and defined product.

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• Chemical & Material Sciences (AREA)
• Life Sciences & Earth Sciences (AREA)
• Biochemistry (AREA)
• Polymers & Plastics (AREA)
• Engineering & Computer Science (AREA)
• Food Science & Technology (AREA)
• Health & Medical Sciences (AREA)
• Organic Chemistry (AREA)
• Nutrition Science (AREA)
• Zoology (AREA)
• Medicinal Chemistry (AREA)
• Chemical Kinetics & Catalysis (AREA)
• Genetics & Genomics (AREA)
• Biophysics (AREA)
• General Health & Medical Sciences (AREA)
• Analytical Chemistry (AREA)
• Molecular Biology (AREA)
• Proteomics, Peptides & Aminoacids (AREA)
• General Chemical & Material Sciences (AREA)
• Water Supply & Treatment (AREA)
• Peptides Or Proteins (AREA)
• Cosmetics (AREA)
• Preparation Of Compounds By Using Micro-Organisms (AREA)

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• 2011
  • 2011-11-30 DE DE102011055889A patent/DE102011055889B4/de not_active Expired - Fee Related
• 2012
  • 2012-11-30 BR BR112014012814A patent/BR112014012814A8/pt not_active Application Discontinuation
  • 2012-11-30 CN CN201280056218.8A patent/CN103957724B/zh not_active Expired - Fee Related
  • 2012-11-30 IN IN3060DEN2014 patent/IN2014DN03060A/en unknown
  • 2012-11-30 JP JP2014542733A patent/JP6164697B2/ja not_active Expired - Fee Related
  • 2012-11-30 WO PCT/EP2012/004940 patent/WO2013079208A1/de not_active Ceased
  • 2012-11-30 EP EP12798159.5A patent/EP2785197A1/de not_active Withdrawn
  • 2012-11-30 US US14/355,453 patent/US20140323702A1/en not_active Abandoned

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