WO2023061981A1 - Procédé de production d'un hydrolysat - Google Patents

Procédé de production d'un hydrolysat Download PDF

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Publication number
WO2023061981A1
WO2023061981A1 PCT/EP2022/078191 EP2022078191W WO2023061981A1 WO 2023061981 A1 WO2023061981 A1 WO 2023061981A1 EP 2022078191 W EP2022078191 W EP 2022078191W WO 2023061981 A1 WO2023061981 A1 WO 2023061981A1
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WO
WIPO (PCT)
Prior art keywords
fish scale
enzyme composition
hydrolysate
protease
process according
Prior art date
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PCT/EP2022/078191
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English (en)
Inventor
Yang Chen
Zhong-Hua QUAN
Ying ZHA
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Dsm Ip Assets B.V.
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Publication date
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Publication of WO2023061981A1 publication Critical patent/WO2023061981A1/fr

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    • 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
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
    • A23J1/001—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from waste materials, e.g. kitchen waste
    • A23J1/002—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from waste materials, e.g. kitchen waste from animal waste materials
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
    • A23J1/10—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from hair, feathers, horn, skins, leather, bones, or the like
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J3/00—Working-up of proteins for foodstuffs
    • A23J3/04—Animal proteins
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J3/00—Working-up of proteins for foodstuffs
    • A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
    • A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
    • 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
    • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
    • A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
    • A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
    • A23L33/17—Amino acids, peptides or proteins
    • A23L33/18—Peptides; Protein hydrolysates
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K8/00—Cosmetics or similar toiletry preparations
    • A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
    • A61K8/96—Cosmetics or similar toiletry preparations characterised by the composition containing materials, or derivatives thereof of undetermined constitution
    • A61K8/98—Cosmetics or similar toiletry preparations characterised by the composition containing materials, or derivatives thereof of undetermined constitution of animal origin
    • A61K8/987—Cosmetics or similar toiletry preparations characterised by the composition containing materials, or derivatives thereof of undetermined constitution of animal origin of species other than mammals or birds
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
    • A61Q19/00—Preparations for care of the skin
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K2800/00—Properties of cosmetic compositions or active ingredients thereof or formulation aids used therein and process related aspects
    • A61K2800/10—General cosmetic use

Definitions

  • the present invention generally relates to the fields of enzymology and industrial hydrolysate production. Particularly, the present invention relates to processes for producing hydrolysates. More particularly, the present invention relates to enzymes and their use in processes for producing hydrolysates.
  • Fish scales constitute about 5% of the fish waste. They are known to be a rich source of valuable components including proteins such as gelatin, collagen and chitin which are important components in food and biomedical industries.
  • An object of the invention is a process for producing fish scale hydrolysates by using enzymes. Optimization and improvement lie inter alia in the pretreatment as well as the enzymes used in the process.
  • the invention relates to a process for producing a fish scale hydrolysate comprising the steps of (a) pretreating fish scale for 1 to 60 minutes at a temperature ranging from 80°C to 120°C and a pH ranging from 5 to 12 and (b) adding at least a first enzyme composition to the pretreated fish scale and incubating the obtained mixture for 1 to 5 hours at a temperature ranging from 40°C to 70°C to obtain the fish scale hydrolysate.
  • the fish scale is removed from the fish.
  • the removal of fish scale is called descaling.
  • Descaling can be performed manually. However, large fish processing industries make use of descaling processes wherein automated fish descaling machinery is used.
  • the fish scale can be derived from marine as well as freshwater fish. Examples include, but are not limited to, bonito, mackerel, drum, sea bass, tuna, swordfish, anchoveta, herring, shad, skipjack, yellowfin and pompano.
  • the fish scale may be washed first with either processing, tap, distilled or de-ionised water to remove dusts, dirt and other unwanted particles.
  • the fish scale is washed first with an alkaline solution and then with water to rinse.
  • the fish scale is decalcified. Decalcification is done before pretreatment by washing the fish scale with acid and then with an alkaline solution.
  • the pretreatment of the fish scale is done in a reactor.
  • the pretreatment may also be done in two, three, four, five, six, seven, eight, nine, ten or even more reactors.
  • the term “reactor” is not limited to a single reactor but may mean multiple reactors.
  • the pretreatment is done in a reactor having a volume of 0.5 - 200 m 3 , preferably of 1 - 100 m 3 .
  • multiple reactors are used in the pretreatment of the processes as described herein, they may have the same volume, but also may have a different volume.
  • the incubation of the obtained mixture of the first enzyme composition and pretreated fish scale is done in a reactor.
  • the incubation may also be done in two, three, four, five, six, seven, eight, nine, ten or even more reactors.
  • the term “reactor” is not limited to a single reactor but may mean multiple reactors.
  • the enzymatic incubation is done in a reactor having a volume of 0.5 - 200 m 3 , preferably of 1 - 100 m 3 .
  • multiple reactors are used in the enzymatic incubation of the processes as described herein, they may have the same volume, but also may have a different volume.
  • the pretreatment and the enzymatic incubation are performed in the same reactor(s). In another embodiment they are performed in separate reactors.
  • pretreated fish scale is added to the reactor in which the enzymatic incubation takes place. This can be done batch-wise, fed-batch wise or continuously.
  • the first enzyme composition is added to the reactor in which the enzymatic incubation takes place. This can be done batch-wise, fed-batch wise or continuously.
  • the first enzyme composition comprises a protease.
  • the first enzyme composition comprises at least one protease.
  • the first enzyme composition may also comprise more than one protease, for example two, three, four, five, six or even more different proteases.
  • the first enzyme composition may be an aqueous composition.
  • protease as used herein is defined as an enzyme that hydrolyses peptide bonds. It includes any enzyme belonging to the EC 3.4 enzyme group (including each of the subclasses thereof). The EC number refers to Enzyme Nomenclature from NC-IUBMB which is regularly supplemented and updated. Proteases are also called peptidases, proteinases, peptide hydrolases or proteolytic enzymes. The term protease includes not only natural derived or wildtype proteases but also mutants, variants, fragments etc. thereof exhibiting protease activity, as well as synthetic proteases, such as shuffled proteases, and consensus proteases. Such genetically engineered proteases can be prepared by methods generally known in the art.
  • the first enzyme composition comprises an alkaline protease and/or a neutral protease.
  • the first enzyme composition may comprise an alkaline protease or the first enzyme composition may comprise a neutral protease or the first enzyme composition may comprise an alkaline protease and a neutral protease.
  • the first enzyme composition may comprise more than one alkaline protease and/or more than one neutral protease.
  • the alkaline proteases may differ from one another.
  • the neutral proteases may differ from one another.
  • neutral protease is intended to be an enzyme classified according to the Enzyme Commission number EC 3.4.24.28. Neutral proteases are active at neutral pH.
  • alkaline protease is intended to be an enzyme classified according to the Enzyme Commission number EC 3.4.21 .62. Alkaline proteases are active at neutral to alkaline pH.
  • At least a second enzyme composition is added to the pretreated fish scale.
  • the second enzyme composition is added together with the first enzyme composition to the pretreated fish scale.
  • the second enzyme composition is added to the pretretaed fish scale after the first enzyme composition has been added to the pretreated fish scale.
  • the second enzyme composition may be an aqueous composition.
  • the second enzyme composition is added during incubation.
  • the second enzyme composition is added at least 1 minute, at least 2 minutes, at least 3 minutes, at least 4 minutes, at least 5 minutes, at least 6 minutes, at least 7 minutes, at least 8 minutes, at least 9 minutes, at least 10 minutes, at least 15 minutes, at least 20 minutes, at least 25 minutes, at least 30 minutes, at least 35 minutes, at least 40 minutes, at least 45 minutes, at least 50 minutes, at least 55 minutes, at least 60 minutes, at least 70 minutes, at least 80 minutes, at least 90 minutes, at least 100 minutes, at least 120 minutes, at least 150 minutes, at least 180 minutes, at least 210 minutes, at least 240 minutes, at least 270 minutes, after the start of the incubation.
  • the second enzyme composition comprises a protease.
  • the second enzyme composition comprises at least one protease.
  • the second enzyme composition may also comprise more than one protease, for example two, three, four, five, six or even more different proteases.
  • the second enzyme composition comprises an alkaline protease and/or a neutral protease.
  • the second enzyme composition may comprise an alkaline protease or the second enzyme composition may comprise a neutral protease or the second enzyme composition may comprise an alkaline protease and a neutral protease.
  • the second enzyme composition may comprise more than one alkaline protease and/or more than one neutral protease.
  • the alkaline proteases may differ from one another.
  • the neutral proteases may differ from one another.
  • protease(s) in the first enzyme composition differ from the protease(s) in the second enzyme composition. In an embodiment the protease(s) in the first enzyme composition are the same as the protease(s) in the second enzyme composition.
  • the first enzyme composition and/or the second enzyme composition comprises additional enzymes.
  • additional enzymes can be selected from the group consisting of acetyl esterases, alpha-galactosidases, alpha-glucanases, alpha-glucosidases, aminopeptidases, amylases, arabinases, arabinofuranosidases, asparaginases, betagalactosidases, beta-glucosidases, carbohydrases, carbonic anhydrases, carboxypeptidases, catalases, cellulases, chitinases, chymosins, cutinases, cyclodextrin glycosyltransferases, deoxyribonucleases, endoglucanases, epimerases, esterases, expansins, glucan lysases, glucoamylases, glucose oxidases, glucuronidases, glycosyl hydrolases, hem
  • the pH during pretreatment is ranging from 5 to 12. In other words, the pH during pretreatment is in the range of 5 to 12. In an embodiment the pH during pretreatment is in the range of 6 to 11 . In an embodiment the pH during pretreatment is in the range of 7 to 11 .
  • the temperature during pretreatment is ranging from 80°C to 120°C. In other words, the temperature during pretreatment is in the range of 80°C to 120°C. In an embodiment the temperature during pretreatment is in the range of 85°C to 115°C. In an embodiment the temperature during pretreatment is in the range of 90°C to 110°C. In an embodiment the temperature during pretreatment i: in the range of 95°C to 105°C
  • the pretreatment is done for 1 to 60 minutes. In an embodiment pretreatment is done for
  • pretreatment is done for 10 to 50 minutes. In an embodiment pretreatment is done for 15 to 45 minutes. In an embodiment pretreatment is done for 20 to 40 minutes.
  • the temperature during incubation is ranging from 40°C to 70°C. In other words, the temperature during incubation is in the range of 40°C to 70°C. In an embodiment the temperature during incubation is in the range of 45°C to 65°C. In an embodiment the temperature during incubation is in the range of 50°C to 60°C. In an embodiment the temperature during incubation is in the range of 52°C to 58°C. In an embodiment the temperature during incubation is in the range of 54°C to 56°C.
  • the incubation is done for 1 to 5 hours. In an embodiment incubation is done for 1 .5 to 4.5 hours. In an embodiment incubation is done for 2 to 4 hours.
  • the first enzyme composition is added at a dosage ranging from 0.1% to 2.0% (w/w pretreated fish scale (dry matter)). In an embodiment the first enzyme composition is added at a dosage ranging from 0.2% to 1.8% (w/w pretreated fish scale (dry matter)). In an embodiment the first enzyme composition is added at a dosage ranging from 0.3% to 1 .7% (w/w pretreated fish scale (dry matter)). In an embodiment the first enzyme composition is added at a dosage ranging from 0.4% to 1 .6% (w/w pretreated fish scale (dry matter)).
  • the second enzyme composition is added at a dosage ranging from 0.1 % to 2.0% (w/w pretreated fish scale dry matter). In an embodiment the second enzyme composition is added at a dosage ranging from 0.2% to 1 .8% (w/w pretreated fish scale dry matter). In an embodiment the second enzyme composition is added at a dosage ranging from 0.3% to 1 .7% (w/w pretreated fish scale dry matter). In an embodiment the second enzyme composition is added at a dosage ranging from 0.4% to 1 .6% (w/w pretreated fish scale dry matter).
  • the process as described herein further comprises adjusting the pH of the fish scale before pretreatment to a pH ranging from 7 to 11 . If needed, additional pH adjustment is done during pretreatment. In an embodiment pH adjustment is done by adding a hydroxide of an alkali metal and/or a hydroxide of an alkaline earth metal to the fish scale.
  • the hydroxide of an alkali metal and/or the hydroxide of an alkaline earth metal are selected from the group consisting of aluminium hydroxide, barium hydroxide, calcium hydroxide, caesium hydroxide, potassium hydroxide, lithium hydroxide, magnesium hydroxide, sodium hydroxide, rubidium hydroxide, strontium hydroxide and any combination thereof.
  • the hydroxide is sodium hydroxide.
  • the fish scale hydrolysate may be subjected to one or more purification steps using methods known in the art such as centrifugation, decantation, plate filtration, frame filtration, microfiltration, ultrafiltration and nanofiltration.
  • the fish scale hydrolysate and/or the specific compounds and/or fractions extracted from the fish scale hydrolysate may be dried. Drying can be done by means of known technologies such as spray drying, freeze drying and roller drum drying. Before drying, the fish scale hydrolysate and/or the specific compounds and/or fractions extracted from the fish scale hydrolysate may be concentrated.
  • the present invention also relates to a fish scale hydrolysate obtainable by a process as described herein. All embodiments and features described above for the process for producing a fish scale hydrolysate also apply to the fish scale hydrolysate obtainable by a process as described herein.
  • the fish scale hydrolysate as described herein comprises peptides.
  • the term “peptides” as used herein means short chains of amino acids, typically comprising 2-50 amino acids. The amino acids in a peptide are connected to one another in a sequence by bonds called peptide bonds.
  • the fish scale hydrolysate as described herein comprises peptides comprising a molecular weight of 5 kD or lower. In an embodiment at least 80% of the peptides in the fish scale hydrolysate as described herein comprise a molecular weight of 5 kD or lower. In an embodiment at least 85% of the peptides in the fish scale hydrolysate as described herein comprise a molecular weight of 5 kD or lower.
  • At least 90% of the peptides in the fish scale hydrolysate as described herein comprise a molecular weight of 5 kD or lower. In an embodiment at least 91 % of the peptides in the fish scale hydrolysate as described herein comprise a molecular weight of 5 kD or lower. In an embodiment at least 92% of the peptides in the fish scale hydrolysate as described herein comprise a molecular weight of 5 kD or lower. In an embodiment at least 93% of the peptides in the fish scale hydrolysate as described herein comprise a molecular weight of 5 kD or lower.
  • At least 94% of the peptides in the fish scale hydrolysate as described herein comprise a molecular weight of 5 kD or lower. In an embodiment at least 95% of the peptides in the fish scale hydrolysate as described herein comprise a molecular weight of 5 kD or lower. In an embodiment at least 96% of the peptides in the fish scale hydrolysate as described herein comprise a molecular weight of 5 kD or lower. In an embodiment at least 97% of the peptides in the fish scale hydrolysate as described herein comprise a molecular weight of 5 kD or lower.
  • At least 98% of the peptides in the fish scale hydrolysate as described herein comprise a molecular weight of 5 kD or lower. In an embodiment at least 99% of the peptides in the fish scale hydrolysate as described herein comprise a molecular weight of 5 kD or lower. In an embodiment 100% of the peptides in the fish scale hydrolysate as described herein comprise a molecular weight of 5 kD or lower.
  • molecular weight distribution analysis methods can be applied.
  • the following molecular weight distribution analysis method is used.
  • the sample is gellated, it is first heated to liquidize the gel. Liquid samples are kept at room temperature. After homogenization on a vortex stirrer (Scientific Industries G- 560E), approximately 50 mg of each sample is mixed with approximately 4950 pl 100 mM sodium phosphate buffer + 400 mM sodium chloride pH 6.4. The added buffer volume is adjusted to the sample weight to obtain a 100 times (w/v) dilution of each sample. The diluted samples are centrifuged for 15 minutes at 20000xg at room temperature (Eppendorf 5417C).
  • Size exclusion chromatography (SEC) profiles are recorded using ultraviolet (UV) detection at 214 nm.
  • Standards bovine serum albumin (Sigma P0914), ovalbumin (Bio-Rad 151 1901), equine myoglobin (Bio-Rad 1511901), [Glu]-fibrinopeptide B (Sigma F3261), glutathione oxidized (Sigma G4376), and glutathione reduced (G4251) are injected to calibrate the column and to assign molecular weight fractions of >50 kDa, 15-50 kDa, 5-15 kDa, 1 - 5 kDa and ⁇ 1 kDa. The peak areas of each molecular weight fraction of the hydrolyzate samples are exported and evaluated.
  • a fish scale hydrolysate as described herein comprises peptides in range of 1 to 20% (w/w). In an embodiment a fish scale hydrolysate as described herein comprises peptides in range of 2 to 18% (w/w). In an embodiment a fish scale hydrolysate as described herein comprises peptides in range of 3 to 16% (w/w). In an embodiment a fish scale hydrolysate as described herein comprises peptides in range of 4 to 14% (w/w). In an embodiment a fish scale hydrolysate as described herein comprises peptides in range of 5 to 12% (w/w). In an embodiment a fish scale hydrolysate as described herein comprises peptides in range of 6 to 10% (w/w).
  • a fish scale hydrolysate as described herein comprises a protease.
  • a fish scale hydrolysate as described herein comprises at least one protease.
  • the fish scale hydrolysate may also comprise more than one protease, for example two, three, four, five, six or even more different proteases. The one or more proteases in the fish scale hydrolysate are inactivated.
  • the fish scale hydrolysate comprises an alkaline protease and/or a neutral protease.
  • the fish scale hydrolysate may comprise an alkaline protease or the fish scale hydrolysate may comprise a neutral protease or the fish scale hydrolysate may comprise an alkaline protease and a neutral protease.
  • the fish scale hydrolysate may comprise more than one alkaline protease and/or more than one neutral protease.
  • the alkaline proteases may differ from one another.
  • the neutral proteases may differ from one another.
  • the fish scale hydrolysate as described herein may also comprise at least one compounds selected from the group consisting of collagen, fat, lecithin, sclerotin, vitamin, gelatin, hydroxyapatite, guanine, chitin, chitosan, mucopolysaccharides, calcium phosphate, magnesium, iron, zinc and calcium.
  • the fish scale hydrolysate is a powder.
  • the present invention also relates to a food, feed, pharmaceutical, cosmetic, biomedical or biosorbent product comprising a fish scale hydrolysate as described herein. All embodiments and features described above for the process for producing a fish scale hydrolysate and/or all embodiments and features described above for the fish scale hydrolysate of the invention also apply to the food, feed, pharmaceutical, cosmetic, biomedical or biosorbent product as described herein.
  • the vials were placed in a water bath and pretreated under the conditions as shown in Table 1 .
  • the samples were subjected to enzymatic hydrolysis.
  • the vials were placed in ice or boiling water to quickly reach the appropriate temperatures for incubation.
  • enzymes were added to the vials and incubated in a water bath during 3 hours under the conditions as shown in Table 2.
  • the enzymes used were Sqzyme PS-KL, an alkaline protease (pH optimum 7-12 from Suntaq) and Maxipro NPU, a neutral protease (pH optimum 5-8 from DSM).
  • the samples were subjected to enzymatic hydrolysis.
  • the vials were placed in ice water to quickly reach the incubation temperature of 55°C.
  • enzymes were added to the vials and incubated in a water bath during 3 hours under the conditions as shown in Table 4.
  • the enzymes used were Sqzyme PS-KL, an alkaline protease (pH optimum 7-12 from Suntaq) and Sqzyme PS-NL, a neutral protease (pH optimum 5.5-9 from Suntaq).
  • the samples were subjected to enzymatic hydrolysis.
  • the vials were placed in ice water to quickly reach the incubation temperature of 50°C.
  • enzymes were added to the vials and incubated in a water bath during 3 hours under the conditions as shown in Table 6.
  • the enzymes used were Alcalase 2.4L, an alkaline protease (pH optimum 6-12 from Novozymes) and Maxipro NPU, a neutral protease (pH optimum 5-8 from DSM).
  • Table 7 The data in Table 7 show that increasing the pH during pretreatment leads to higher extraction yields on total solids.
  • Table 1 Pretreatment conditions during fish scale hydrolysate production process.
  • Table 2 Temperatures and enzymes applied during enzymatic hydrolysis.
  • Table 3 Brix value of samples.
  • Table 4 Temperatures, pH and enzymes applied during enzymatic hydrolysis.
  • Table 5 Brix value of samples. Table 6. Temperatures, pH and enzymes applied during fish scale hydrolysate production process.

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Abstract

La présente invention concerne un procédé de production d'un hydrolysat par utilisation d'enzymes.
PCT/EP2022/078191 2021-10-14 2022-10-11 Procédé de production d'un hydrolysat WO2023061981A1 (fr)

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CNPCT/CN2021/123816 2021-10-14
EP21207442 2021-11-10
EP21207442.1 2021-11-10

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Publication number Priority date Publication date Assignee Title
CN102613383B (zh) * 2012-04-24 2015-04-15 天津春宇食品配料有限公司 一种鱼鳞蛋白酶解液及其制备方法
CN104140992B (zh) * 2013-11-26 2018-10-09 国家海洋局第三海洋研究所 一种鱼鳞ⅰ型胶原蛋白肽的规模化制备方法
CN111345339A (zh) * 2020-03-20 2020-06-30 江西师范大学 一种草鱼鱼鳞明胶水解物抗冻剂的制备方法
CN109371082B (zh) * 2018-10-29 2021-06-18 浙江海洋大学 一种罗非鱼鱼鳞免疫调节肽的制备方法

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CN102613383B (zh) * 2012-04-24 2015-04-15 天津春宇食品配料有限公司 一种鱼鳞蛋白酶解液及其制备方法
CN104140992B (zh) * 2013-11-26 2018-10-09 国家海洋局第三海洋研究所 一种鱼鳞ⅰ型胶原蛋白肽的规模化制备方法
CN109371082B (zh) * 2018-10-29 2021-06-18 浙江海洋大学 一种罗非鱼鱼鳞免疫调节肽的制备方法
CN111345339A (zh) * 2020-03-20 2020-06-30 江西师范大学 一种草鱼鱼鳞明胶水解物抗冻剂的制备方法

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Title
IZZATI H ET AL: "Low Molecular Weight Collagen from Tilapia Fish Scales for Potential Cosmetic Application", DER CHEMICA CHEMICA, 1 January 2017 (2017-01-01), pages 108 - 114, XP055912263, Retrieved from the Internet <URL:https://www.derpharmachemica.com/pharma-chemica/low-molecular-weight-collagen-from-tilapia-fish-scales-for-potential-cosmetic-application.pdf> [retrieved on 20220413] *
ZHANG YIQI ET AL: "Fish Scale Valorization by Hydrothermal Pretreatment Followed by Enzymatic Hydrolysis for Gelatin Hydrolysate Production", MOLECULES, vol. 24, no. 16, 19 August 2019 (2019-08-19), pages 2998, XP055912121, DOI: 10.3390/molecules24162998 *

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