CN116211733B - Preparation method of whitening composite protein peptide enzymatic hydrolysate - Google Patents
Preparation method of whitening composite protein peptide enzymatic hydrolysate Download PDFInfo
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- CN116211733B CN116211733B CN202310177744.XA CN202310177744A CN116211733B CN 116211733 B CN116211733 B CN 116211733B CN 202310177744 A CN202310177744 A CN 202310177744A CN 116211733 B CN116211733 B CN 116211733B
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- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 108
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 78
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 78
- 230000002087 whitening effect Effects 0.000 title claims abstract description 36
- 230000002255 enzymatic effect Effects 0.000 title claims abstract description 29
- 238000002360 preparation method Methods 0.000 title claims abstract description 13
- 239000000413 hydrolysate Substances 0.000 title claims description 20
- 239000002131 composite material Substances 0.000 title claims description 10
- 240000006162 Chenopodium quinoa Species 0.000 claims abstract description 106
- 241000251468 Actinopterygii Species 0.000 claims abstract description 88
- 108010035532 Collagen Proteins 0.000 claims abstract description 40
- 102000008186 Collagen Human genes 0.000 claims abstract description 40
- 229920001436 collagen Polymers 0.000 claims abstract description 40
- 102000004190 Enzymes Human genes 0.000 claims abstract description 33
- 108090000790 Enzymes Proteins 0.000 claims abstract description 33
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 33
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 claims abstract description 28
- 229920001184 polypeptide Polymers 0.000 claims abstract description 25
- QIGBRXMKCJKVMJ-UHFFFAOYSA-N Hydroquinone Chemical compound OC1=CC=C(O)C=C1 QIGBRXMKCJKVMJ-UHFFFAOYSA-N 0.000 claims abstract description 20
- 239000002994 raw material Substances 0.000 claims abstract description 14
- 150000001875 compounds Chemical class 0.000 claims abstract description 12
- 108010009736 Protein Hydrolysates Proteins 0.000 claims abstract description 9
- 239000010902 straw Substances 0.000 claims abstract description 9
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 claims description 78
- 239000007788 liquid Substances 0.000 claims description 64
- 239000000243 solution Substances 0.000 claims description 63
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 claims description 58
- 238000003756 stirring Methods 0.000 claims description 54
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 51
- 238000010438 heat treatment Methods 0.000 claims description 49
- 238000002156 mixing Methods 0.000 claims description 49
- 238000001914 filtration Methods 0.000 claims description 38
- 239000012153 distilled water Substances 0.000 claims description 37
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 35
- 239000006228 supernatant Substances 0.000 claims description 34
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 29
- 238000001816 cooling Methods 0.000 claims description 28
- 239000012065 filter cake Substances 0.000 claims description 25
- 230000000415 inactivating effect Effects 0.000 claims description 24
- 238000002791 soaking Methods 0.000 claims description 22
- VYQNWZOUAUKGHI-UHFFFAOYSA-N monobenzone Chemical compound C1=CC(O)=CC=C1OCC1=CC=CC=C1 VYQNWZOUAUKGHI-UHFFFAOYSA-N 0.000 claims description 21
- YMWUJEATGCHHMB-UHFFFAOYSA-N Dichloromethane Chemical compound ClCCl YMWUJEATGCHHMB-UHFFFAOYSA-N 0.000 claims description 20
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 claims description 18
- 239000011259 mixed solution Substances 0.000 claims description 16
- 238000005406 washing Methods 0.000 claims description 16
- 238000001035 drying Methods 0.000 claims description 15
- 239000011780 sodium chloride Substances 0.000 claims description 15
- 239000007787 solid Substances 0.000 claims description 15
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 claims description 14
- 108091005658 Basic proteases Proteins 0.000 claims description 13
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 claims description 12
- 108090000145 Bacillolysin Proteins 0.000 claims description 11
- 102000035092 Neutral proteases Human genes 0.000 claims description 11
- 108091005507 Neutral proteases Proteins 0.000 claims description 11
- 238000000034 method Methods 0.000 claims description 11
- VHYFNPMBLIVWCW-UHFFFAOYSA-N 4-Dimethylaminopyridine Chemical compound CN(C)C1=CC=NC=C1 VHYFNPMBLIVWCW-UHFFFAOYSA-N 0.000 claims description 10
- 238000004587 chromatography analysis Methods 0.000 claims description 10
- 239000008367 deionised water Substances 0.000 claims description 10
- 229910021641 deionized water Inorganic materials 0.000 claims description 10
- 239000012528 membrane Substances 0.000 claims description 10
- 108091005804 Peptidases Proteins 0.000 claims description 8
- 239000004365 Protease Substances 0.000 claims description 8
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims description 8
- 230000002378 acidificating effect Effects 0.000 claims description 8
- 239000002244 precipitate Substances 0.000 claims description 8
- 239000003607 modifier Substances 0.000 claims description 6
- 238000010025 steaming Methods 0.000 claims description 6
- 239000000126 substance Substances 0.000 claims description 6
- 238000000967 suction filtration Methods 0.000 claims description 6
- 238000009210 therapy by ultrasound Methods 0.000 claims description 6
- UFHFLCQGNIYNRP-UHFFFAOYSA-N Hydrogen Chemical compound [H][H] UFHFLCQGNIYNRP-UHFFFAOYSA-N 0.000 claims description 5
- CSNNHWWHGAXBCP-UHFFFAOYSA-L Magnesium sulfate Chemical compound [Mg+2].[O-][S+2]([O-])([O-])[O-] CSNNHWWHGAXBCP-UHFFFAOYSA-L 0.000 claims description 5
- KCXMKQUNVWSEMD-UHFFFAOYSA-N benzyl chloride Chemical compound ClCC1=CC=CC=C1 KCXMKQUNVWSEMD-UHFFFAOYSA-N 0.000 claims description 5
- 229940073608 benzyl chloride Drugs 0.000 claims description 5
- 150000001718 carbodiimides Chemical class 0.000 claims description 5
- 239000000706 filtrate Substances 0.000 claims description 5
- UKVIEHSSVKSQBA-UHFFFAOYSA-N methane;palladium Chemical compound C.[Pd] UKVIEHSSVKSQBA-UHFFFAOYSA-N 0.000 claims description 5
- 238000005185 salting out Methods 0.000 claims description 5
- 230000008961 swelling Effects 0.000 claims description 5
- 241000276707 Tilapia Species 0.000 claims description 4
- 238000011010 flushing procedure Methods 0.000 claims description 4
- 108091005508 Acid proteases Proteins 0.000 claims description 3
- 239000001257 hydrogen Substances 0.000 claims description 3
- 229910052739 hydrogen Inorganic materials 0.000 claims description 3
- 239000013049 sediment Substances 0.000 claims description 3
- 238000005119 centrifugation Methods 0.000 claims description 2
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- 210000003491 skin Anatomy 0.000 description 77
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- 102000003425 Tyrosinase Human genes 0.000 description 11
- 108060008724 Tyrosinase Proteins 0.000 description 11
- WTDRDQBEARUVNC-LURJTMIESA-N L-DOPA Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C(O)=C1 WTDRDQBEARUVNC-LURJTMIESA-N 0.000 description 7
- 229910052799 carbon Inorganic materials 0.000 description 6
- 238000002835 absorbance Methods 0.000 description 5
- XUMBMVFBXHLACL-UHFFFAOYSA-N Melanin Chemical compound O=C1C(=O)C(C2=CNC3=C(C(C(=O)C4=C32)=O)C)=C2C4=CNC2=C1C XUMBMVFBXHLACL-UHFFFAOYSA-N 0.000 description 4
- 239000000203 mixture Substances 0.000 description 4
- 239000012488 sample solution Substances 0.000 description 4
- 238000012360 testing method Methods 0.000 description 4
- 238000005303 weighing Methods 0.000 description 4
- 150000001413 amino acids Chemical class 0.000 description 3
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 3
- 230000005764 inhibitory process Effects 0.000 description 3
- 210000002752 melanocyte Anatomy 0.000 description 3
- 238000005374 membrane filtration Methods 0.000 description 3
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N phenol group Chemical group C1(=CC=CC=C1)O ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 3
- 239000000049 pigment Substances 0.000 description 3
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- AHMIDUVKSGCHAU-UHFFFAOYSA-N Dopaquinone Natural products OC(=O)C(N)CC1=CC(=O)C(=O)C=C1 AHMIDUVKSGCHAU-UHFFFAOYSA-N 0.000 description 2
- AHMIDUVKSGCHAU-LURJTMIESA-N L-dopaquinone Chemical compound [O-]C(=O)[C@@H]([NH3+])CC1=CC(=O)C(=O)C=C1 AHMIDUVKSGCHAU-LURJTMIESA-N 0.000 description 2
- 238000006555 catalytic reaction Methods 0.000 description 2
- 210000002421 cell wall Anatomy 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 230000002349 favourable effect Effects 0.000 description 2
- 229920005610 lignin Polymers 0.000 description 2
- 229920002521 macromolecule Polymers 0.000 description 2
- 230000036564 melanin content Effects 0.000 description 2
- 230000035790 physiological processes and functions Effects 0.000 description 2
- 238000002390 rotary evaporation Methods 0.000 description 2
- 239000000523 sample Substances 0.000 description 2
- 102100030310 5,6-dihydroxyindole-2-carboxylic acid oxidase Human genes 0.000 description 1
- 101710163881 5,6-dihydroxyindole-2-carboxylic acid oxidase Proteins 0.000 description 1
- 108010082495 Dietary Plant Proteins Proteins 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 125000001797 benzyl group Chemical group [H]C1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])* 0.000 description 1
- 230000000975 bioactive effect Effects 0.000 description 1
- 239000011203 carbon fibre reinforced carbon Chemical group 0.000 description 1
- 125000002915 carbonyl group Chemical group [*:2]C([*:1])=O 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- BNIILDVGGAEEIG-UHFFFAOYSA-L disodium hydrogen phosphate Chemical compound [Na+].[Na+].OP([O-])([O-])=O BNIILDVGGAEEIG-UHFFFAOYSA-L 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 235000019441 ethanol Nutrition 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 230000009931 harmful effect Effects 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 229910000403 monosodium phosphate Inorganic materials 0.000 description 1
- 235000019799 monosodium phosphate Nutrition 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 230000000144 pharmacologic effect Effects 0.000 description 1
- 239000008055 phosphate buffer solution Substances 0.000 description 1
- 125000006239 protecting group Chemical group 0.000 description 1
- 210000004511 skin melanocyte Anatomy 0.000 description 1
- AJPJDKMHJJGVTQ-UHFFFAOYSA-M sodium dihydrogen phosphate Chemical compound [Na+].OP(O)([O-])=O AJPJDKMHJJGVTQ-UHFFFAOYSA-M 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 230000001502 supplementing effect Effects 0.000 description 1
- 238000010257 thawing Methods 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 239000002699 waste material Substances 0.000 description 1
Classifications
-
- 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
- A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
- A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
- A61K8/65—Collagen; Gelatin; Keratin; Derivatives or degradation products thereof
-
- 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
- A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
- A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
- A61K8/645—Proteins of vegetable origin; Derivatives or degradation products thereof
-
- 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
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q19/00—Preparations for care of the skin
- A61Q19/02—Preparations for care of the skin for chemically bleaching or whitening the skin
-
- 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
- A61Q19/08—Anti-ageing preparations
-
- 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
- A61K2800/40—Chemical, physico-chemical or functional or structural properties of particular ingredients
- A61K2800/52—Stabilizers
- A61K2800/522—Antioxidants; Radical scavengers
-
- 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
- A61K2800/40—Chemical, physico-chemical or functional or structural properties of particular ingredients
- A61K2800/59—Mixtures
- A61K2800/592—Mixtures of compounds complementing their respective functions
-
- 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
- A61K2800/74—Biological properties of particular ingredients
- A61K2800/78—Enzyme modulators, e.g. Enzyme agonists
- A61K2800/782—Enzyme inhibitors; Enzyme antagonists
-
- 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
- A61K2800/80—Process related aspects concerning the preparation of the cosmetic composition or the storage or application thereof
- A61K2800/805—Corresponding aspects not provided for by any of codes A61K2800/81 - A61K2800/95
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02P—CLIMATE CHANGE MITIGATION TECHNOLOGIES IN THE PRODUCTION OR PROCESSING OF GOODS
- Y02P60/00—Technologies relating to agriculture, livestock or agroalimentary industries
- Y02P60/80—Food processing, e.g. use of renewable energies or variable speed drives in handling, conveying or stacking
- Y02P60/87—Re-use of by-products of food processing for fodder production
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Veterinary Medicine (AREA)
- Animal Behavior & Ethology (AREA)
- General Health & Medical Sciences (AREA)
- Public Health (AREA)
- Dermatology (AREA)
- Birds (AREA)
- Epidemiology (AREA)
- Gerontology & Geriatric Medicine (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Cosmetics (AREA)
Abstract
The invention discloses a preparation method of a whitening compound protein peptide enzymatic hydrolysate, and relates to the technical field of protein peptides. The invention firstly utilizes hydrogen peroxide to pretreat the quinoa bran and quinoa straw, which is beneficial to the entry of extracting solution and the dissolution of quinoa protein, and then adopts compound enzyme to respectively carry out graded enzymolysis treatment on quinoa protein and fishskin collagen to obtain micromolecular polypeptide, thereby improving the yield of polypeptide and further enhancing the whitening activity of enzymolysis solution; and then carrying out coupling modification on the fish skin collagen peptide by using hydroquinone, improving the whitening effect of the fish skin collagen peptide, and compounding the fish skin collagen peptide with quinoa polypeptide to realize synergistic interaction and deep absorption of whitening active substances. The invention adopts natural substances as raw materials, is safe and has no toxic or side effect, and can realize the whitening effect.
Description
Technical Field
The invention relates to the technical field of protein peptides, in particular to a preparation method of whitening compound protein peptide enzymatic hydrolysate.
Background
The skin tone is mainly determined by the number of skin melanocytes and the amount of cellular melanin. The skin appears white when the melanocyte ratio is small and the melanin content is low. The skin appears dark when the melanocyte ratio is large and the melanin content is high. In melanocytes, tyrosine is oxidized to dopa and dopa quinone in sequence under the catalysis of tyrosinase, dopa quinone is further converted to dopa pigment, and dopa pigment gradually forms melanin under the catalysis of DHI enzyme, dopa pigment tautomerase and DHICA oxidase.
The bioactive peptide is peptide matter with special physiological function, and is peptide segment with 2-20 amino acids length and specific bioactivity prepared through enzyme hydrolysis, etc. and may be released from parent protein through in vivo or in vitro enzymolysis to perform specific physiological function. Compared with chemical synthetic medicines, the food-borne and vegetable protein peptide has the advantages of safety, no toxic or side effect and the like. In the existing research on preparation methods of quinoa peptide and collagen peptide, active peptide is mainly extracted by a single enzymolysis method, however, the single enzymolysis method is easy to have the defects of insufficient enzymolysis, high molecular weight of the obtained active peptide, low whitening activity and the like.
Disclosure of Invention
The invention aims to provide a preparation method of whitening compound protein peptide enzymatic hydrolysate, which aims to solve the problems in the prior art.
In order to solve the technical problems, the invention provides the following technical scheme: the whitening composite protein peptide enzymatic hydrolysate comprises quinoa polypeptide enzymatic hydrolysate and fish skin collagen peptide modified matters.
Further, the quinoa polypeptide enzymatic hydrolysate is prepared by performing hydrogen peroxide pretreatment on quinoa bran and quinoa straw and then performing fractional enzymolysis.
Further, the fish skin collagen peptide modifier is prepared by extracting fish skin protein from fish skin through sodium chloride solution and citric acid, carrying out fractional enzymolysis to obtain fish skin collagen peptide enzymolysis liquid, and then coupling with hydroquinone.
Further, the fish skin is one or more of Anhui fish skin, tilapia fish skin or cod fish skin.
Further, the preparation method of the whitening composite protein peptide enzymatic hydrolysate comprises the following preparation steps:
(1) Mixing pretreated quinoa and distilled water according to a feed liquid ratio of 1:15, carrying out ultrasonic treatment at 25kHz for 40-50 min, centrifuging at 4000rpm for 10min, taking supernatant, carrying out rotary steaming at 160rpm for 10-16 min at 50 ℃ under 0.084MPa of vacuum degree to obtain mixed liquid, adding absolute ethyl alcohol with the volume of 3-4 times of that of the mixed liquid, standing for 30min, centrifuging at 5000rpm for 25-35 min, and taking precipitate to obtain quinoa protein;
(2) Mixing quinoa protein and distilled water according to a feed-liquid ratio of 1:10, uniformly stirring, and carrying out fractional enzymolysis to obtain quinoa polypeptide enzymolysis liquid;
(3) Cutting the fish skin into small pieces with the length of 2 multiplied by 2cm by a knife, flushing the small pieces with distilled water for 3 to 5 times, soaking the small pieces in distilled water with the weight of 20 to 34 times of the fish skin, taking out the fish skin after soaking the small pieces for 24 hours, soaking the fish skin in a sodium chloride solution according to the mass ratio of 1:10, taking out the fish skin after stirring the small pieces for 12 hours at 100rpm at the temperature of 5 ℃ with the mass ratio of 3:100, soaking the fish skin in citric acid according to the mass ratio of 1:30, swelling the small pieces for 24 hours at 800 rpm for 3 minutes, filtering the small pieces, salting out the small pieces until the concentration of the sodium chloride is 4mol/L, standing the small pieces at the temperature of 4 ℃ for 24 hours at 600 rpm for 15 minutes, and taking out sediment to obtain fish skin protein;
(4) Mixing fish skin protein and distilled water according to a feed-liquid ratio of 1:9, uniformly stirring, and carrying out fractional enzymolysis to obtain fish skin collagen peptide enzymatic hydrolysate;
(5) Mixing p-benzyloxy phenol, fish skin collagen peptide enzymatic hydrolysate, 4-dimethylaminopyridine and methylene dichloride according to the mass ratio of 1:2:1.0:30-1:3:1.3:35, cooling to 0 ℃, adding carbodiimide with the mass of 1.8-2.0 times of that of p-benzyloxy phenol and methylene dichloride with the mass of 30-35 times of that of p-benzyloxy phenol, stirring for 5-10 min at 60rpm, heating to room temperature, continuing stirring for 2-4 h, heating to 40 ℃, heating for 3-5 h, extracting, washing for 5-7 times by using saturated sodium chloride solution to obtain mixed solution, adding anhydrous magnesium sulfate with the mass of 0.1 times of that of the mixed solution, drying for 8-12 h, filtering, and performing chromatography to obtain an intermediate;
(6) Mixing the intermediate, absolute ethyl alcohol and palladium-carbon according to the mass ratio of 1:22:0.05-1:27:0.1, stirring at 70rpm for 6-8 hours under the hydrogen atmosphere, filtering, taking filtrate, distilling for 1.5-3 hours under the vacuum degree of 0.085MPa and the temperature of 55 ℃, and carrying out chromatography to obtain the fish skin collagen peptide modified substance; and mixing quinoa polypeptide enzymolysis liquid and the fish skin collagen peptide modifier according to the mass ratio of 2:1 to obtain the whitening compound protein peptide enzymolysis liquid.
Further, the preparation method of the pretreated quinoa in the step (1) comprises the following steps: mixing quinoa raw material and hydrogen peroxide solution according to a feed liquid ratio of 1:10-1:18, wherein the mass ratio of hydrogen peroxide to deionized water in the hydrogen peroxide solution is 4:100-8:100, adding sodium hydroxide to the solution until the pH value is 7.0, soaking for 1.5-2.5 h at 75-85 ℃, centrifuging at 6000rpm for 8min, taking solid, and drying at 50 ℃ for 6h.
Further, the quinoa raw material is that quinoa bran and quinoa straw are mixed according to the mass ratio of 1:1-1:3, and crushed to 80-100 meshes by a crusher.
Further, the step (2) and the step (4) are carried out as follows: adding sodium hydroxide to the pH value of the solution to be 8, adding alkaline protease with the protein quantity of 0.00075-0.001 times, carrying out enzymolysis for 2-4 hours at 50 ℃, heating to 90 ℃, inactivating enzyme for 20-30 minutes, cooling to 50 ℃, adding hydrochloric acid to the pH value of the solution to be 6.5, adding neutral protease with the protein quantity of 0.0005-0.001 times, carrying out enzymolysis for 1-3 hours, heating to 90 ℃, inactivating enzyme for 20-30 minutes, cooling to 45 ℃, adding hydrochloric acid to the pH value of 2.8, adding acidic protease with the protein quantity of 0.0005-0.001 times, carrying out enzymolysis for 1-2 hours, heating to 90 ℃, inactivating enzyme for 20-30 minutes, centrifuging, decolorizing, and filtering.
Further, the centrifugation step is: centrifuging at 4500-6000 rpm for 20-30 min, and collecting supernatant; the decoloring step comprises the following steps: adding activated carbon with the supernatant of 0.01-0.03 times of the mass and diatomite with the supernatant of 0.01-0.03 times of the mass, and decoloring for 40-60 min at 50-60 ℃ at 30-50 rpm; the filtering steps are as follows: the membrane was passed through a 3kD membrane having a filtration area of 30cm 2 under a pressure of 0.15MPa and a stirring speed of 120 rpm.
Further, the preparation method of the p-benzyloxy phenol in the step (5) comprises the following steps: mixing absolute ethyl alcohol, deionized water and sodium hydroxide according to the mass ratio of 1:0.6:0.1, stirring and dissolving, heating to 75 ℃, adding hydroquinone with the mass of 0.2-0.4 times of the absolute ethyl alcohol, stirring at 80rpm for 10-15 min, adding benzyl chloride with the mass of 0.2-0.3 times of the absolute ethyl alcohol, continuing to react for 50-70 min, distilling at the vacuum degree of 0.085MPa and 55 ℃ for 2-3h, cooling to room temperature, adding hydrochloric acid until solid is completely separated out, carrying out suction filtration, taking a filter cake, placing the filter cake into a sodium hydroxide solution with the mass fraction of 17% and the mass fraction of 1-3 times of the filter cake, stirring at 80rpm for 20-30 min, carrying out suction filtration, taking the filter cake, adding hydrochloric acid until the solid is not separated out, carrying out suction filtration, taking the filter cake, washing with distilled water until the pH of a washing liquid is 7, and drying at 40 ℃ for 8h, thus obtaining p-benzyloxy phenol.
Compared with the prior art, the invention has the following beneficial effects:
The composite peptide enzymatic hydrolysate prepared by the invention contains quinoa polypeptide enzymatic hydrolysate and fish skin collagen peptide modified matters, has high safety, is natural, has no chemical reagent residue, is safe and free from toxic and side effects, does not have harmful effects on human bodies, and can realize the effects of whitening and high purity.
Firstly, fresh quinoa bran and quinoa straw are adopted as raw materials, pretreatment is carried out, hydrogen peroxide reacts with carbonyl groups and carbon-carbon double bonds on lignin side chains in quinoa cell walls, lignin is rapidly hydrolyzed, so that the cell walls are damaged, the entry of an extracting solution and the dissolution of quinoa protein are facilitated, and then alkaline protease, neutral protease and acid protease are adopted to carry out first graded enzymolysis treatment on quinoa protein, so that quinoa protein macromolecules can be fully hydrolyzed into small molecular weight protein peptides, the generation of low molecular weight amino acids is reduced, small molecular quinoa peptides can be efficiently obtained, the yield and purity of the quinoa peptides are improved, the whitening property and the oxidation resistance of the obtained quinoa peptides are higher, waste resources are effectively utilized, and a new idea is provided for the development of various pharmacological active substances.
Secondly, after the fish skin is subjected to secondary fractional enzymolysis treatment, fish skin collagen peptide is obtained, and has the effects of supplementing water, preserving moisture and relieving, and can drive quinoa polypeptide to realize deep absorption, so as to synergistically increase the whitening effect of the composite protein peptide enzymolysis liquid; and then, introducing a benzyl protecting group into the phenolic hydroxyl group on one side of hydroquinone to prevent the hydroquinone from reacting completely and losing the whitening activity, removing the protecting group after the phenolic hydroxyl group on the other side is coupled with the fish skin collagen peptide, improving the whitening effect of the composite protein peptide enzymatic hydrolysate by the combined action of the phenolic hydroxyl group on the other side and the quinoa polypeptide, and simultaneously, having no stimulation to skin and small toxic and side effects.
Detailed Description
The technical solutions of the embodiments of the present invention will be clearly and completely described below in conjunction with the embodiments of the present invention, and it is apparent that the described embodiments are only some embodiments of the present invention, not all embodiments. All other embodiments, which can be made by those skilled in the art based on the embodiments of the invention without making any inventive effort, are intended to be within the scope of the invention.
In order to more clearly illustrate the method provided by the invention, the following examples are used for describing the detailed description, and the method for testing each index of the whitening composite protein peptide enzymatic hydrolysate, the quinoa polypeptide and the fishskin collagen peptide prepared in the following examples is as follows:
Yield is as follows: performing rotary evaporation and concentration on quinoa polypeptide enzymolysis liquid and fish skin collagen peptide enzymolysis liquid, adding absolute ethyl alcohol to ensure that the volume fraction of the ethyl alcohol is 80%, standing for 30min, centrifuging at 5000rpm for 30min, taking supernatant, performing rotary evaporation and concentration, performing freeze drying, and determining by using a Kjeldahl nitrogen method in GB/T5009.5; yield = content in crude polypeptide/content of protein in quinoa (fish skin) ×100%.
Whitening: performing tyrosinase inhibition efficiency test on the examples and the comparative examples with the same mass; respectively weighing 3.12g of sodium dihydrogen phosphate and 7.16g of disodium hydrogen phosphate, dissolving in distilled water, then, fixing the volume to 100mL by using distilled water, and mixing in a volume ratio of 51:49 to obtain PBS solution; weighing 1380U/mg tyrosinase, dissolving in phosphate buffer solution to prepare 100U/mL tyrosinase solution, preserving at-20deg.C in dark, thawing at 4deg.C before use, weighing 0.26mL tyrosinase solution before use, using brown volumetric flask, and adding PBS solution to volume to 10mL; 0.150g of dopa is weighed, 1mL of hydrochloric acid with the concentration of 0.1mol/L is used for dissolution, and then PBS solution is added to prepare 1.5mg/mL of dopa solution; weighing 0.6g of each example and each comparative example, and preparing sample liquid with the mass concentration of 0.5mg/mL by using ionized water; then adding the reagents into each group of test tubes respectively according to the following table, carrying out water bath for 10min at 37 ℃, then rapidly adding 1mL of dopa solution into each group of test tubes respectively, continuing to carry out water bath for 5min at 37 ℃, transferring into a cuvette, and measuring the absorbance of the cuvette at 475 nm;
Tyrosinase inhibition ratio= [1- (a T1-AT2)/(AC1-AC2) ] ×100%
Wherein A C1 is absorbance of the mixed solution when the quinoa peptide sample solution is not added and the tyrosinase solution is added; a C2 is absorbance of the mixed solution when no quinoa peptide sample solution and no tyrosinase solution are added; a T1 is absorbance of the mixed solution when quinoa peptide sample solution and tyrosinase solution are added simultaneously; a T2 is absorbance of the mixed solution when quinoa peptide sample solution is added and tyrosinase solution is not added.
| Reaction set | VPBS(mL) | V Sample liquid (mL) | V Enzyme solution (mL) |
| C1 | 1.5 | 0 | 0.5 |
| C2 | 2 | 0 | 0 |
| T1 | 1 | 0.5 | 0.5 |
| T2 | 1.5 | 0.5 | 0 |
Example 1
(1) Mixing quinoa bran and quinoa straw according to a mass ratio of 1:1, and crushing the mixture to a sieve of 80 meshes by using a crusher to obtain quinoa raw materials; mixing quinoa raw material and a hydrogen peroxide solution according to a feed liquid ratio of 1:10, wherein the mass ratio of hydrogen peroxide to deionized water in the hydrogen peroxide solution is 4:100, adding sodium hydroxide to the solution until the pH is 7, soaking at 75 ℃ for 1.5 hours, centrifuging at 6000rpm for 8 minutes, taking solid, and drying at 50 ℃ for 6 hours to obtain pretreated quinoa;
(2) Mixing pretreated quinoa and distilled water according to a feed liquid ratio of 1:15, carrying out ultrasonic treatment at 25kHz for 40min, centrifuging at 4000rpm for 10min, taking supernatant, carrying out rotary steaming at 160rpm for 10min at 50 ℃ under 0.084MPa of vacuum degree to obtain mixed liquid, adding absolute ethyl alcohol with 3 times of the volume of the mixed liquid, standing for 30min, centrifuging at 5000rpm for 25min, and taking precipitate to obtain quinoa protein;
(3) Mixing quinoa protein and distilled water according to a feed liquid ratio of 1:10, stirring uniformly, adding sodium hydroxide to a solution pH of 8, adding alkaline protease with the weight of 0.00075 times of quinoa protein, carrying out enzymolysis for 2 hours at 50 ℃, heating to 90 ℃, inactivating enzyme for 20 minutes, cooling to 50 ℃, adding hydrochloric acid to a solution pH of 6.5, adding neutral protease with the weight of 0.0005 times of quinoa protein, carrying out enzymolysis for 1 hour, heating to 90 ℃ and inactivating enzyme for 20 minutes, cooling to 45 ℃, adding hydrochloric acid to a pH of 2.8, adding acidic protease with the weight of 0.0005 times of quinoa protein, carrying out enzymolysis for 1 hour, heating to 90 ℃, inactivating enzyme for 20 minutes, centrifuging for 20 minutes at 4500rpm, taking supernatant, adding active carbon with the weight of 0.01 times of supernatant and diatomite with the weight of 0.01 times of diatomite, decolorizing for 40 minutes at 50 ℃ and 30rpm, and obtaining quinoa polypeptide enzymatic hydrolysate through a membrane with the filtration area of 2 and 3kD under the conditions of 0.15MPa and 120 rpm;
(4) Cutting tilapia skin into small pieces with the length of 2X 2cm by a knife, flushing 3 times by distilled water, soaking in distilled water with the weight of 20 times of the cortex of the tilapia skin, taking out the skin, soaking in sodium chloride solution according to the mass ratio of 1:10, wherein the mass ratio of sodium chloride to distilled water in the sodium chloride solution is 3:100,5 ℃, stirring at 100rpm for 12 hours, taking out the skin, soaking in citric acid according to the mass ratio of 1:30, swelling for 24 hours, 80 rpm for 3 minutes, filtering, salting out until the concentration of sodium chloride is 4mol/L, standing for 24 hours at the temperature of 4 ℃ and centrifuging for 15 minutes at 600 rpm, and taking out sediment to obtain fish skin protein;
(5) Mixing fish skin protein and distilled water according to a feed liquid ratio of 1:9, stirring uniformly, adding sodium hydroxide to the pH of the solution to 8, adding alkaline protease with the fish skin protein content of 0.00075 times, carrying out enzymolysis for 2 hours at 50 ℃, heating to 90 ℃, inactivating enzyme for 20 minutes, cooling to 50 ℃, adding hydrochloric acid to the pH of the solution to 6.5, adding neutral protease with the fish skin protein content of 0.0005 times, carrying out enzymolysis for 1 hour, heating to 90 ℃ to inactivate enzyme for 20 minutes, cooling to 45 ℃, adding hydrochloric acid to the pH of 2.8, adding acidic protease with the fish skin protein content of 0.0005 times, carrying out enzymolysis for 1-2 hours, heating to 90 ℃ to inactivate enzyme for 20 minutes, centrifuging for 20 minutes at 4500rpm, taking supernatant, adding active carbon with the supernatant of 0.01 times, diatomite with the supernatant quality of 0.01 times, decolorizing at 50 ℃ and 30rpm for 40 minutes at a pressure of 0.15MPa and a stirring speed of 120rpm, and passing through a membrane with a filtering area of 30 2 and 3kD, thereby obtaining a fish skin collagen peptide enzymolysis solution;
(6) Mixing absolute ethyl alcohol, deionized water and sodium hydroxide according to the mass ratio of 1:0.6:0.1, stirring and dissolving, heating to 75 ℃, adding hydroquinone with the mass of 0.2 times of absolute ethyl alcohol, stirring at 80rpm for 10min, adding benzyl chloride with the mass of 0.2 times of absolute ethyl alcohol, continuing to react for 50min, distilling at the vacuum degree of 0.085MPa and the temperature of 55 ℃ for 2h, cooling to room temperature, adding hydrochloric acid until solid is completely separated out, suction filtering, taking a filter cake, placing the filter cake into a sodium hydroxide solution with the mass fraction of 17% which is 1 time of the mass of the filter cake, stirring at 80rpm for 20min, suction filtering, taking the filter cake, adding hydrochloric acid until the solid is not separated out, suction filtering, taking the filter cake, washing with distilled water until the pH of a washing liquid is 7, and drying at 40 ℃ for 8h to obtain p-benzyloxy phenol;
(7) Mixing p-benzyloxy phenol, fish skin collagen peptide enzymatic hydrolysate, 4-dimethylaminopyridine and methylene dichloride according to a mass ratio of 1:2:1.0:30, cooling to 0 ℃, adding carbodiimide with the mass of 1.8 times of that of the p-benzyloxy phenol and methylene dichloride with the mass of 30 times of that of the p-benzyloxy phenol, stirring at 60rpm for 5min, heating to room temperature, continuously stirring for 2h, heating to 40 ℃, heating for 3h, extracting, washing with saturated sodium chloride solution for 5 times to obtain a mixed solution, adding anhydrous magnesium sulfate with the mass of 0.1 times of that of the mixed solution, drying for 8h, filtering, and performing chromatography to obtain an intermediate;
(8) Mixing the intermediate, absolute ethyl alcohol and palladium-carbon according to a mass ratio of 1:22:0.05, stirring at 70rpm for 6 hours in a hydrogen gas atmosphere, filtering, taking filtrate, distilling at a vacuum degree of 0.085MPa and a temperature of 55 ℃ for 1.5 hours, and carrying out chromatography to obtain a fish skin collagen peptide modified substance; and mixing quinoa polypeptide enzymolysis liquid and the fish skin collagen peptide modifier according to the mass ratio of 2:1 to obtain the whitening compound protein peptide enzymolysis liquid.
Example 2
(1) Mixing quinoa bran and quinoa straw according to a mass ratio of 1:2, and crushing the mixture to a sieve of 90 meshes by using a crusher to obtain quinoa raw materials; mixing quinoa raw material and a hydrogen peroxide solution according to a feed liquid ratio of 1:14, wherein the mass ratio of hydrogen peroxide to deionized water in the hydrogen peroxide solution is 6:100, adding sodium hydroxide to the solution until the pH is 7.0, soaking at 80 ℃ for 2 hours, centrifuging at 6000rpm for 8 minutes, taking solid, and drying at 50 ℃ for 6 hours to obtain pretreated quinoa;
(2) Mixing pretreated quinoa and distilled water according to a feed liquid ratio of 1:15, carrying out ultrasonic treatment at 25kHz for 45min, centrifuging at 4000rpm for 10min, taking supernatant, carrying out rotary steaming at 160rpm for 13min at 50 ℃ under 0.084MPa to obtain mixed liquid, adding absolute ethyl alcohol with the volume of 3.5 times of that of the mixed liquid, standing for 30min, centrifuging at 5000rpm for 30min, and taking precipitate to obtain quinoa protein;
(3) Mixing quinoa protein and distilled water according to a feed liquid ratio of 1:10, stirring uniformly, adding sodium hydroxide to the pH of the solution to 8, adding alkaline protease with the weight of 0.000875 times of quinoa protein, carrying out enzymolysis at 50 ℃ for 3 hours, heating to 90 ℃, inactivating enzyme for 25 minutes, cooling to 50 ℃, adding hydrochloric acid to the pH of the solution to 6.5, adding neutral protease with the weight of 0.00075 times of quinoa protein, carrying out enzymolysis for 2 hours, heating to 90 ℃ to inactivate enzyme for 25 minutes, cooling to 45 ℃, adding hydrochloric acid to pH of 2.8, adding acidic protease with the weight of 0.00075 times of quinoa protein, carrying out enzymolysis for 1.5 hours, heating to 90 ℃, inactivating enzyme for 25 minutes, centrifuging at 5200rpm for 25 minutes, taking supernatant, adding active carbon with the weight of 0.02 times of supernatant and diatomite with the weight of 0.02 times, decolorizing at 55 ℃ and 40rpm for 50 minutes, and obtaining quinoa polypeptide enzymolysis liquid through a membrane with the filtration area of 30cm 2 and 3kD under the conditions of 0.15MPa and 120 rpm;
(4) Cutting the Anhui fish skin into small pieces with the length of 2 multiplied by 2cm by a knife, flushing 3 to 5 times by distilled water, soaking in distilled water with the length of 27 times of Anhui fish cortex, taking out the fish skin, soaking in a sodium chloride solution according to the mass ratio of 1:10, wherein the mass ratio of sodium chloride to distilled water in the sodium chloride solution is 3:100, the temperature is 5 ℃, stirring at 100rpm for 12 hours, taking out the fish skin, soaking in citric acid according to the mass ratio of 1:30, swelling for 24 hours, homogenizing at 800 rpm for 3 minutes, filtering, salting out until the concentration of sodium chloride is 4mol/L, standing at 4 ℃ for 24 hours, centrifuging at 6000rpm for 15 minutes, and taking out precipitate to obtain fish skin protein;
(5) Mixing fish skin protein and distilled water according to a feed liquid ratio of 1:9, stirring uniformly, adding sodium hydroxide to the pH of the solution to 8, adding alkaline protease with the fish skin protein content of 0.000875 times, carrying out enzymolysis at 50 ℃ for 3 hours, heating to 90 ℃, inactivating enzyme for 25 minutes, cooling to 50 ℃, adding hydrochloric acid to the pH of the solution to 6.5, adding neutral protease with the fish skin protein content of 0.00075 times, carrying out enzymolysis for 2 hours, heating to 90 ℃ to inactivate enzyme for 25 minutes, cooling to 45 ℃, adding hydrochloric acid to the pH of 2.8, adding acidic protease with the fish skin protein content of 0.00075 times, carrying out enzymolysis for 1.5 hours, heating to 90 ℃, inactivating enzyme for 25 minutes, 5200rpm centrifuging for 25 minutes, taking supernatant, adding active carbon with the supernatant of 0.02 times, diatomite with the supernatant of 0.02 times, decolorizing at 55 ℃ and 40rpm for 50 minutes, and carrying out membrane filtration area of 30cm 2 and 3kD under the conditions of a stirring speed of 120rpm, thereby obtaining the fish skin collagen peptide enzymatic hydrolysate;
(6) Mixing absolute ethyl alcohol, deionized water and sodium hydroxide according to the mass ratio of 1:0.6:0.1, stirring and dissolving, heating to 75 ℃, adding hydroquinone with the mass of 0.3 times of absolute ethyl alcohol, stirring at 80rpm for 12min, adding benzyl chloride with the mass of 0.25 times of absolute ethyl alcohol, continuing to react for 60min, distilling at the vacuum degree of 0.085MPa and the temperature of 55 ℃ for 2.5h, cooling to room temperature, adding hydrochloric acid until solid is completely separated out, suction filtering, taking a filter cake, placing the filter cake into sodium hydroxide solution with the mass fraction of 17% with the mass of 2 times of the filter cake, stirring at 80rpm for 25min, suction filtering, taking the filter cake, adding hydrochloric acid until the solid is not separated out, suction filtering, taking the filter cake, washing with distilled water until the pH of a washing liquid is 7, and drying at the temperature of 40 ℃ for 8h to obtain p-benzyloxy phenol;
(7) Mixing p-benzyloxy phenol, fish skin collagen peptide enzymatic hydrolysate, 4-dimethylaminopyridine and methylene dichloride according to the mass ratio of 1:2.5:1.15:32.5, cooling to 0 ℃, adding carbodiimide with the mass of 1.9 times of the p-benzyloxy phenol and methylene dichloride with the mass of 32.5 times of the p-benzyloxy phenol, stirring at 60rpm for 7min, heating to room temperature, continuously stirring for 3h, heating to 40 ℃, heating for 4h, extracting, washing with saturated sodium chloride solution for 6 times to obtain mixed solution, adding anhydrous magnesium sulfate with the mass of 0.1 times of the mixed solution, drying for 10h, filtering, and performing chromatography to obtain an intermediate;
(8) Mixing the intermediate, absolute ethyl alcohol and palladium-carbon according to the mass ratio of 1:24.5:0.075, stirring at 70rpm for 7 hours under the hydrogen atmosphere, filtering, taking filtrate, distilling at the vacuum degree of 0.085MPa and the temperature of 55 ℃ for 2.3 hours, and carrying out chromatography to obtain the fish skin collagen peptide modified substance; and mixing quinoa polypeptide enzymolysis liquid and the fish skin collagen peptide modifier according to the mass ratio of 2:1 to obtain the whitening compound protein peptide enzymolysis liquid.
Example 3
(1) Mixing quinoa bran and quinoa straw according to a mass ratio of 1:3, and crushing the mixture to a sieve of 100 meshes by using a crusher to obtain quinoa raw materials; mixing quinoa raw material and a hydrogen peroxide solution according to a feed liquid ratio of 1:18, wherein the mass ratio of hydrogen peroxide to deionized water in the hydrogen peroxide solution is 8:100, adding sodium hydroxide to the solution until the pH is 7.0, soaking at 85 ℃ for 2.5 hours, centrifuging at 6000rpm for 8 minutes, taking solid, and drying at 50 ℃ for 6 hours to obtain pretreated quinoa;
(2) Mixing pretreated quinoa and distilled water according to a feed liquid ratio of 1:15, carrying out ultrasonic treatment at 25kHz for 50min, centrifuging at 4000rpm for 10min, taking supernatant, carrying out rotary steaming at 160rpm for 16min at 50 ℃ under 0.084MPa of vacuum degree to obtain mixed liquid, adding absolute ethyl alcohol with the volume being 4 times of that of the mixed liquid, standing for 30min, centrifuging at 5000rpm for 35min, and taking precipitate to obtain quinoa protein;
(3) Mixing quinoa protein and distilled water according to a feed liquid ratio of 1:10, stirring uniformly, adding sodium hydroxide to a solution pH of 8, adding alkaline protease with the weight of 0.001 times of quinoa protein, carrying out enzymolysis for 4 hours at 50 ℃, heating to 90 ℃, inactivating enzyme for 30 minutes, cooling to 50 ℃, adding hydrochloric acid to a solution pH of 6.5, adding neutral protease with the weight of 0.001 times of quinoa protein, carrying out enzymolysis for 3 hours, heating to 90 ℃, inactivating enzyme for 30 minutes, cooling to 45 ℃, adding hydrochloric acid to pH of 2.8, adding acidic protease with the weight of 0.001 times of quinoa protein, carrying out enzymolysis for 2 hours, heating to 90 ℃, inactivating enzyme for 30 minutes, centrifuging for 30 minutes at 6000rpm, taking supernatant, adding active carbon with the weight of 0.03 times of supernatant, diatomite with the weight of 0.03 times of diatomite, decolorizing at 60 ℃ at 50rpm for 60 minutes, and carrying out enzymolysis for 3kD membrane with the filtration area of 2 under the conditions of 0.15MPa and 120rpm of stirring speed, so as to obtain quinoa polypeptide enzymatic hydrolysate;
(4) Cutting cod skin into small pieces of 2X 2cm by a knife, washing with distilled water for 5 times, soaking in distilled water with 34 times of the fish skin amount for 24 hours, taking out the fish skin, soaking in sodium chloride solution according to a feed liquid ratio of 1:10, stirring for 12 hours at 100rpm at a temperature of 5 ℃ with the mass ratio of 3:100, taking out the fish skin, soaking in citric acid according to a feed liquid ratio of 1:30, swelling for 24 hours at 800 rpm for 3 minutes, filtering, salting out until the sodium chloride concentration is 4mol/L, standing for 24 hours at 6000rpm for 15 minutes at 4 ℃, and taking out precipitate to obtain fish skin protein;
(5) Mixing fish skin protein and distilled water according to a feed liquid ratio of 1:9, stirring uniformly, adding sodium hydroxide to the pH of the solution to 8, adding alkaline protease with the fish skin protein content of 0.001 times, carrying out enzymolysis for 4 hours at 50 ℃, heating to 90 ℃, inactivating enzyme for 30min, cooling to 50 ℃, adding hydrochloric acid to the pH of the solution to 6.5, adding neutral protease with the fish skin protein content of 0.001 times, carrying out enzymolysis for 3h, heating to 90 ℃ to inactivate enzyme for 30min, cooling to 45 ℃, adding hydrochloric acid to the pH of 2.8, adding acidic protease with the fish skin protein content of 0.001 times, carrying out enzymolysis for 2h, heating to 90 ℃, inactivating enzyme for 30min, centrifuging for 30min at 6000rpm, taking supernatant, adding active carbon with the supernatant of 0.03 times, diatomite with the supernatant quality of 0.03 times, decolorizing for 60 ℃ at 50rpm for 60min, and obtaining the fish skin collagen peptide enzymolysis liquid through a membrane with the filtration area of 30cm 2 and 3kD under the conditions of 0.15MPa and 120 rpm;
(6) Mixing absolute ethyl alcohol, deionized water and sodium hydroxide according to the mass ratio of 1:0.6:0.1, stirring and dissolving, heating to 75 ℃, adding hydroquinone with the mass of 0.4 times of absolute ethyl alcohol, stirring at 80rpm for 15min, adding benzyl chloride with the mass of 0.3 times of absolute ethyl alcohol, continuing to react for 70min, distilling at the vacuum degree of 0.085MPa and the temperature of 55 ℃ for 3h, cooling to room temperature, adding hydrochloric acid until solid is completely separated out, suction filtering, taking a filter cake, placing the filter cake into a sodium hydroxide solution with the mass fraction of 17% with the mass of 3 times of the filter cake, stirring at 80rpm for 30min, suction filtering, taking the filter cake, adding hydrochloric acid until the solid is not separated out, suction filtering, taking the filter cake, washing with distilled water until the pH of a washing liquid is 7, and drying at 40 ℃ for 8h to obtain p-benzyloxy phenol;
(7) Mixing p-benzyloxy phenol, fish skin collagen peptide enzymatic hydrolysate, 4-dimethylaminopyridine and methylene dichloride according to a mass ratio of 1:3:1.3:35, cooling to 0 ℃, adding carbodiimide with 2 times of the mass of the p-benzyloxy phenol and methylene dichloride with 35 times of the mass of the p-benzyloxy phenol, stirring for 10min at 60rpm, heating to room temperature, continuously stirring for 4h, heating to 40 ℃, heating for 5h, extracting, washing with saturated sodium chloride solution for 7 times to obtain mixed solution, adding anhydrous magnesium sulfate with 0.1 time of the mixed solution, drying for 12h, filtering, and carrying out chromatography to obtain an intermediate;
(8) Mixing the intermediate, absolute ethyl alcohol and palladium-carbon according to a mass ratio of 1:27:0.1, stirring at 70rpm for 8 hours in a hydrogen gas atmosphere, filtering, taking filtrate, distilling at a vacuum degree of 0.085MPa and a temperature of 55 ℃ for 3 hours, and carrying out chromatography to obtain a fish skin collagen peptide modified substance; and mixing quinoa polypeptide enzymolysis liquid and the fish skin collagen peptide modifier according to the mass ratio of 2:1 to obtain the whitening compound protein peptide enzymolysis liquid.
Comparative example 1
Comparative example 1 differs from example 2 in that there is no step (1), step (2) is changed to: mixing quinoa bran and quinoa straw according to a mass ratio of 1:2, and crushing the mixture to a sieve of 90 meshes by using a crusher to obtain quinoa raw materials; mixing quinoa raw material and distilled water according to a feed liquid ratio of 1:15, carrying out ultrasonic treatment at 25kHz for 45min, centrifuging at 4000rpm for 10min, taking supernatant, carrying out rotary steaming at 160rpm for 13min at 50 ℃ under 0.084MPa to obtain mixed liquid, adding absolute ethyl alcohol with the volume of 3.5 times of that of the mixed liquid, standing for 30min, centrifuging at 5000rpm for 30min, and taking precipitate to obtain quinoa protein. The rest of the procedure is the same as in example 2.
Comparative example 2
Comparative example 2 differs from example 2 in that step (3) was different, and step (3) was changed to: mixing quinoa protein and distilled water according to a feed liquid ratio of 1:10, stirring uniformly, adding sodium hydroxide to a solution pH of 8, adding alkaline protease with 0.000875 times of quinoa protein mass, carrying out enzymolysis for 3 hours at 50 ℃, heating to 90 ℃, inactivating enzyme for 25 minutes, centrifuging for 25 minutes at 5200rpm, taking supernatant, adding activated carbon with 0.02 times of the supernatant mass and diatomite with 0.02 times of the supernatant mass, decolorizing for 50 minutes at 55 ℃ at 40rpm, and carrying out membrane filtration with a filtration area of 30cm 2 and 3kD under the conditions of a pressure of 0.15MPa and a stirring speed of 120rpm to obtain quinoa polypeptide enzymolysis liquid. The rest of the procedure is the same as in example 2.
Comparative example 3
Comparative example 3 differs from example 2 in that step (5) was changed to: mixing fish skin protein and distilled water according to a feed liquid ratio of 1:9, stirring uniformly, adding sodium hydroxide to a solution pH of 8, adding alkaline protease with 0.000875 times of the amount of the fish skin protein, carrying out enzymolysis for 3 hours at 50 ℃, heating to 90 ℃, inactivating enzyme for 25 minutes, centrifuging at 5200rpm for 25 minutes, taking supernatant, adding activated carbon with 0.02 times of the mass of the supernatant and diatomite with 0.02 times of the mass of the supernatant, decolorizing at 55 ℃ at 40rpm for 50 minutes, and carrying out membrane filtration with a filtration area of 30cm 2 and a membrane with 3kD under the pressure of 0.15MPa and the stirring speed of 120rpm to obtain the fish skin collagen peptide enzymatic hydrolysate. The rest of the procedure is the same as in example 2.
Comparative example 4
Comparative example 4 differs from example 2 in that steps (6), (7) are not present, step (8) is changed to: and mixing quinoa polypeptide enzymolysis liquid and fish skin collagen peptide enzymolysis liquid according to the mass ratio of 2:1 to obtain the whitening compound protein peptide enzymolysis liquid. The rest of the procedure is the same as in example 2.
Comparative example 5
Comparative example 5 was different from example 2 in that there were no steps (4) to (8), and the remaining steps were the same as example 2.
Effect example
The results of the performance analysis of the whitening complex protein peptide enzymatic hydrolysate using examples 1 to 3 and comparative examples 1 to 5 of the present invention are shown in table 1 below.
TABLE 1
As can be found from comparison of experimental data of tyrosinase inhibition rate and peptide yield of the embodiment and the comparative example, the application utilizes hydrogen peroxide to pretreat quinoa, which is favorable for entering extracting solution and dissolving quinoa protein, improves the yield of quinoa polypeptide, indirectly improves the whitening effect of enzymolysis solution, and then adopts alkaline protease, neutral protease and acid protease to carry out fractional enzymolysis treatment on quinoa protein and fish skin collagen respectively, so that protein macromolecules can be fully hydrolyzed into protein peptides with small molecular weight, the generation of low molecular weight amino acid is reduced, small molecular peptides can be efficiently obtained, the yield and purity of quinoa peptide and collagen peptide are improved, thereby being favorable for improving the whitening activity of enzymolysis solution, and meanwhile, the application adopts the combination of the fish skin collagen peptide and quinoa polypeptide to realize deep absorption of whitening active substances and improve the whitening effect of compound protein peptide enzymolysis solution; and then coupling hydroquinone with the fish skin collagen peptide to improve the whitening effect of the fish skin collagen peptide and further enhance the whitening effect of the composite protein peptide enzymatic hydrolysate.
It will be evident to those skilled in the art that the invention is not limited to the details of the foregoing illustrative embodiments, and that the present invention may be embodied in other specific forms without departing from the spirit or essential characteristics thereof. The present embodiments are, therefore, to be considered in all respects as illustrative and not restrictive, the scope of the invention being indicated by the appended claims rather than by the foregoing description, and all changes which come within the meaning and range of equivalency of the claims are therefore intended to be embraced therein. Any reference sign in a claim should not be construed as limiting the claim concerned.
Claims (4)
1. The preparation method of the whitening composite protein peptide enzymatic hydrolysate is characterized by comprising the following preparation steps:
(1) Mixing quinoa raw material and a hydrogen peroxide solution according to a feed liquid ratio of 1:10-1:18, wherein the mass ratio of hydrogen peroxide to deionized water in the hydrogen peroxide solution is 4:100-8:100, adding sodium hydroxide to the solution until the pH value is 7.0, soaking at 75-85 ℃ for 1.5-2.5 h, centrifuging at 6000rpm for 8min, taking solid, and drying at 50 ℃ for 6h to obtain pretreated quinoa; mixing pretreated quinoa and distilled water according to a feed liquid ratio of 1:15, carrying out ultrasonic treatment at 25kHz for 40-50 min, centrifuging at 4000rpm for 10min, taking supernatant, carrying out rotary steaming at 160rpm for 10-16 min at a vacuum degree of 0.084MPa and 50 ℃ to obtain a mixed solution, adding absolute ethyl alcohol with a volume of 3-4 times that of the mixed solution, standing for 30min, centrifuging at 5000rpm for 25-35 min, and taking precipitate to obtain quinoa protein;
(2) Mixing quinoa protein and distilled water according to a feed liquid ratio of 1:10, stirring uniformly, adding sodium hydroxide to a solution pH of 8, adding alkaline protease with the mass of 0.00075-0.001 times that of quinoa protein, carrying out enzymolysis for 2-4 hours at 50 ℃, heating to 90 ℃, inactivating enzyme for 20-30 minutes, cooling to 50 ℃, adding hydrochloric acid to a solution pH of 6.5, adding neutral protease with the mass of 0.0005-0.001 times that of quinoa protein, carrying out enzymolysis for 1-3 hours, heating to 90 ℃, inactivating enzyme for 20-30 minutes, cooling to 45 ℃, adding hydrochloric acid to a pH of 2.8, adding acidic protease with the mass of 0.0005-0.001 times that of quinoa protein, carrying out enzymolysis for 1-2 hours, heating to 90 ℃, inactivating enzyme for 20-30 minutes, centrifuging, decolorizing, and filtering to obtain quinoa polypeptide enzymolysis liquid;
(3) Cutting the fish skin into small pieces with the length of 2 multiplied by 2cm by a knife, flushing the small pieces with distilled water for 3 to 5 times, soaking the small pieces in distilled water with the length of 20 to 34 times of the fish skin, taking out the fish skin after soaking for 24 hours, soaking the fish skin in a sodium chloride solution according to the mass ratio of 1:10, taking out the fish skin after stirring the fish skin for 12 hours at 100rpm at the temperature of 5 ℃ with the mass ratio of 3:100, soaking the fish skin in citric acid according to the mass ratio of 1:30, swelling for 24 hours at 800 rpm for 3 minutes, filtering, salting out until the concentration of sodium chloride is 4mol/L, standing for 24 hours at 6000rpm for 15 minutes at the temperature of 4 ℃, and taking out sediment to obtain fish skin protein;
(4) Mixing fish skin protein and distilled water according to a feed liquid ratio of 1:9, stirring uniformly, adding sodium hydroxide to a solution pH of 8, adding alkaline protease with the fish skin protein content of 0.00075-0.001 times, carrying out enzymolysis for 2-4 hours at 50 ℃, heating to 90 ℃, inactivating enzyme for 20-30 minutes, cooling to 50 ℃, adding hydrochloric acid to a solution pH of 6.5, adding neutral protease with the fish skin protein content of 0.0005-0.001 times, carrying out enzymolysis for 1-3 hours, heating to 90 ℃, inactivating enzyme for 20-30 minutes, cooling to 45 ℃, adding hydrochloric acid to a pH of 2.8, adding acid protease with the fish skin protein content of 0.0005-0.001 times, carrying out enzymolysis for 1-2 hours, heating to 90 ℃, inactivating enzyme for 20-30 minutes, centrifuging, decolorizing, and filtering to obtain a fish skin collagen peptide enzymolysis solution;
(5) Mixing absolute ethyl alcohol, deionized water and sodium hydroxide according to a mass ratio of 1:0.6:0.1, stirring and dissolving, heating to 75 ℃, adding hydroquinone with the mass of 0.2-0.4 times of the absolute ethyl alcohol, stirring at 80rpm for 10-15 min, adding benzyl chloride with the mass of 0.2-0.3 times of the absolute ethyl alcohol, continuing to react for 50-70 min, distilling at the vacuum degree of 0.085MPa and 55 ℃ for 2-3 h, cooling to room temperature, adding hydrochloric acid until solid is completely separated out, carrying out suction filtration, taking a filter cake, placing the filter cake into a sodium hydroxide solution with the mass fraction of 17% with the mass fraction of 1-3 times of the filter cake, stirring at 80rpm for 20-30 min, carrying out suction filtration, taking the filter cake, adding hydrochloric acid until the solid is not separated out, carrying out suction filtration, taking the filter cake, washing with distilled water until the pH of a washing liquid is 7, and drying at 40 ℃ for 8h to obtain p-benzyloxy phenol; mixing p-benzyloxy phenol, fish skin collagen peptide enzymatic hydrolysate, 4-dimethylaminopyridine and methylene dichloride according to the mass ratio of 1:2:1.0:30-1:3:1.3:35, cooling to 0 ℃, adding carbodiimide with the mass of 1.8-2.0 times of that of p-benzyloxy phenol and methylene dichloride with the mass of 30-35 times of that of p-benzyloxy phenol, stirring for 5-10 min at 60rpm, heating to room temperature, continuously stirring for 2-4 h, heating to 40 ℃, heating for 3-5 h, extracting, washing for 5-7 times by using saturated sodium chloride solution to obtain mixed solution, adding anhydrous magnesium sulfate with the mass of 0.1 times of that of the mixed solution, drying for 8-12 h, filtering, and performing chromatography to obtain an intermediate;
(6) Mixing the intermediate, absolute ethyl alcohol and palladium-carbon according to a mass ratio of 1:22:0.05-1:27:0.1, stirring at 70rpm for 6-8 hours under a hydrogen atmosphere, filtering, taking filtrate, distilling at a vacuum degree of 0.085MPa and a temperature of 55 ℃ for 1.5-3 hours, and performing chromatography to obtain a fish skin collagen peptide modified substance; and mixing quinoa polypeptide enzymolysis liquid and the fish skin collagen peptide modifier according to the mass ratio of 2:1 to obtain the whitening compound protein peptide enzymolysis liquid.
2. The preparation method of the whitening compound protein peptide enzymatic hydrolysate, which is characterized in that the quinoa raw material in the step (1) is that quinoa bran and quinoa straw are mixed according to a mass ratio of 1:1-1:3, and crushed to 80-100 meshes by using a crusher.
3. The method for preparing the whitening complex protein peptide enzymatic hydrolysate according to claim 1, wherein the centrifugation step in the steps (2) and (4) is as follows: centrifuging at 4500-6000 rpm for 20-30 min, and collecting supernatant; the decoloring step comprises the following steps: adding activated carbon with the mass of 0.01-0.03 times of the supernatant and diatomite with the mass of 0.01-0.03 times of the supernatant, and decoloring at 50-60 ℃ for 40-60 min at 30-50 rpm; the filtering steps are as follows: the membrane was passed through a 3kD membrane having a filtration area of 30cm 2 under a pressure of 0.15MPa and a stirring speed of 120 rpm.
4. The method for preparing the whitening complex protein peptide enzymatic hydrolysate according to claim 1, wherein the fish skin in the step (3) is one or more of Anhui fish skin, tilapia fish skin and cod fish skin.
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| Publication number | Priority date | Publication date | Assignee | Title |
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| CN104073540A (en) * | 2014-07-05 | 2014-10-01 | 广东润科生物工程有限公司 | Polypeptide production method for enhancing utilization ratio of protein |
| CN106638089A (en) * | 2016-09-27 | 2017-05-10 | 济南米铎碳新能源科技有限公司 | Method for preparing dissolving pulp and other high-value-added products by crop straws |
| CN111574618A (en) * | 2020-06-26 | 2020-08-25 | 润科生物工程（福建）有限公司 | Preparation method of whitening compound protein peptidase hydrolysate, whitening compound protein peptide beverage and preparation method thereof |
| CN113337563A (en) * | 2021-06-01 | 2021-09-03 | 科丽思化妆品（上海）有限公司 | Quinoa peptide with whitening and antioxidant activities and preparation method and application thereof |
| CN114807284A (en) * | 2022-06-17 | 2022-07-29 | 徐培 | Preparation method of high-purity small-molecule fish skin collagen peptide |
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Patent Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN104073540A (en) * | 2014-07-05 | 2014-10-01 | 广东润科生物工程有限公司 | Polypeptide production method for enhancing utilization ratio of protein |
| CN106638089A (en) * | 2016-09-27 | 2017-05-10 | 济南米铎碳新能源科技有限公司 | Method for preparing dissolving pulp and other high-value-added products by crop straws |
| CN111574618A (en) * | 2020-06-26 | 2020-08-25 | 润科生物工程（福建）有限公司 | Preparation method of whitening compound protein peptidase hydrolysate, whitening compound protein peptide beverage and preparation method thereof |
| CN113337563A (en) * | 2021-06-01 | 2021-09-03 | 科丽思化妆品（上海）有限公司 | Quinoa peptide with whitening and antioxidant activities and preparation method and application thereof |
| CN114807284A (en) * | 2022-06-17 | 2022-07-29 | 徐培 | Preparation method of high-purity small-molecule fish skin collagen peptide |
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