CN109275916A - A kind of collagen polypeptide powder and preparation method thereof - Google Patents
A kind of collagen polypeptide powder and preparation method thereof Download PDFInfo
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- CN109275916A CN109275916A CN201811539403.8A CN201811539403A CN109275916A CN 109275916 A CN109275916 A CN 109275916A CN 201811539403 A CN201811539403 A CN 201811539403A CN 109275916 A CN109275916 A CN 109275916A
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- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 152
- 108010035532 Collagen Proteins 0.000 title claims abstract description 80
- 102000008186 Collagen Human genes 0.000 title claims abstract description 80
- 229920001436 collagen Polymers 0.000 title claims abstract description 79
- 239000000843 powder Substances 0.000 title claims abstract description 43
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 32
- 229920001184 polypeptide Polymers 0.000 title claims abstract description 29
- 238000002360 preparation method Methods 0.000 title claims description 16
- 241000251511 Holothuroidea Species 0.000 claims abstract description 31
- 235000009496 Juglans regia Nutrition 0.000 claims abstract description 26
- 241000209140 Triticum Species 0.000 claims abstract description 26
- 235000021307 Triticum Nutrition 0.000 claims abstract description 26
- 240000008042 Zea mays Species 0.000 claims abstract description 26
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 claims abstract description 26
- 235000002017 Zea mays subsp mays Nutrition 0.000 claims abstract description 26
- 235000005822 corn Nutrition 0.000 claims abstract description 26
- 235000020234 walnut Nutrition 0.000 claims abstract description 26
- 244000068988 Glycine max Species 0.000 claims abstract description 21
- 235000010469 Glycine max Nutrition 0.000 claims abstract description 21
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 claims abstract description 21
- GSSMIHQEWAQUPM-AOLPDKKJSA-N ovalbumin peptide Chemical compound C([C@H](NC(=O)[C@H](C(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)[C@@H](C)CC)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(O)=O)C1=CN=CN1 GSSMIHQEWAQUPM-AOLPDKKJSA-N 0.000 claims abstract description 19
- BJEPYKJPYRNKOW-REOHCLBHSA-N (S)-malic acid Chemical compound OC(=O)[C@@H](O)CC(O)=O BJEPYKJPYRNKOW-REOHCLBHSA-N 0.000 claims abstract description 11
- BJEPYKJPYRNKOW-UHFFFAOYSA-N alpha-hydroxysuccinic acid Natural products OC(=O)C(O)CC(O)=O BJEPYKJPYRNKOW-UHFFFAOYSA-N 0.000 claims abstract description 11
- 239000001630 malic acid Substances 0.000 claims abstract description 11
- 235000011090 malic acid Nutrition 0.000 claims abstract description 11
- UEDUENGHJMELGK-HYDKPPNVSA-N Stevioside Chemical compound O([C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1O[C@]12C(=C)C[C@@]3(C1)CC[C@@H]1[C@@](C)(CCC[C@]1([C@@H]3CC2)C)C(=O)O[C@H]1[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O1)O)[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O UEDUENGHJMELGK-HYDKPPNVSA-N 0.000 claims abstract description 10
- 229940013618 stevioside Drugs 0.000 claims abstract description 10
- OHHNJQXIOPOJSC-UHFFFAOYSA-N stevioside Natural products CC1(CCCC2(C)C3(C)CCC4(CC3(CCC12C)CC4=C)OC5OC(CO)C(O)C(O)C5OC6OC(CO)C(O)C(O)C6O)C(=O)OC7OC(CO)C(O)C(O)C7O OHHNJQXIOPOJSC-UHFFFAOYSA-N 0.000 claims abstract description 10
- 235000019202 steviosides Nutrition 0.000 claims abstract description 10
- 239000002994 raw material Substances 0.000 claims abstract description 7
- 230000002255 enzymatic effect Effects 0.000 claims abstract description 6
- 241000251468 Actinopterygii Species 0.000 claims abstract description 3
- 108010038807 Oligopeptides Proteins 0.000 claims abstract description 3
- 102000015636 Oligopeptides Human genes 0.000 claims abstract description 3
- 238000002955 isolation Methods 0.000 claims abstract description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 33
- 230000007071 enzymatic hydrolysis Effects 0.000 claims description 25
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 claims description 25
- 241000758789 Juglans Species 0.000 claims description 24
- 238000000034 method Methods 0.000 claims description 24
- 108091005804 Peptidases Proteins 0.000 claims description 19
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- 235000019419 proteases Nutrition 0.000 claims description 19
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- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 claims description 12
- 239000012153 distilled water Substances 0.000 claims description 12
- 230000007062 hydrolysis Effects 0.000 claims description 12
- 238000006460 hydrolysis reaction Methods 0.000 claims description 12
- 240000007594 Oryza sativa Species 0.000 claims description 10
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- 239000002253 acid Substances 0.000 claims description 10
- 235000009566 rice Nutrition 0.000 claims description 10
- 102000004190 Enzymes Human genes 0.000 claims description 9
- 108090000790 Enzymes Proteins 0.000 claims description 9
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 claims description 9
- 239000000796 flavoring agent Substances 0.000 claims description 9
- 235000019634 flavors Nutrition 0.000 claims description 9
- QCVGEOXPDFCNHA-UHFFFAOYSA-N 5,5-dimethyl-2,4-dioxo-1,3-oxazolidine-3-carboxamide Chemical compound CC1(C)OC(=O)N(C(N)=O)C1=O QCVGEOXPDFCNHA-UHFFFAOYSA-N 0.000 claims description 6
- 108090000145 Bacillolysin Proteins 0.000 claims description 6
- 229920000858 Cyclodextrin Polymers 0.000 claims description 6
- 108010000912 Egg Proteins Proteins 0.000 claims description 6
- 102000002322 Egg Proteins Human genes 0.000 claims description 6
- 239000001116 FEMA 4028 Substances 0.000 claims description 6
- MVORZMQFXBLMHM-QWRGUYRKSA-N Gly-His-Lys Chemical compound NCCCC[C@@H](C(O)=O)NC(=O)[C@@H](NC(=O)CN)CC1=CN=CN1 MVORZMQFXBLMHM-QWRGUYRKSA-N 0.000 claims description 6
- 108091005507 Neutral proteases Proteins 0.000 claims description 6
- 102000035092 Neutral proteases Human genes 0.000 claims description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 6
- WHGYBXFWUBPSRW-FOUAGVGXSA-N beta-cyclodextrin Chemical compound OC[C@H]([C@H]([C@@H]([C@H]1O)O)O[C@H]2O[C@@H]([C@@H](O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O3)[C@H](O)[C@H]2O)CO)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O)[C@@H]3O[C@@H]1CO WHGYBXFWUBPSRW-FOUAGVGXSA-N 0.000 claims description 6
- 235000011175 beta-cyclodextrine Nutrition 0.000 claims description 6
- 229960004853 betadex Drugs 0.000 claims description 6
- 150000001875 compounds Chemical class 0.000 claims description 6
- 230000009849 deactivation Effects 0.000 claims description 6
- 235000014103 egg white Nutrition 0.000 claims description 6
- 210000000969 egg white Anatomy 0.000 claims description 6
- 239000000706 filtrate Substances 0.000 claims description 6
- 108010038983 glycyl-histidyl-lysine Proteins 0.000 claims description 6
- 239000012535 impurity Substances 0.000 claims description 6
- 238000001179 sorption measurement Methods 0.000 claims description 6
- 239000006228 supernatant Substances 0.000 claims description 6
- 235000019764 Soybean Meal Nutrition 0.000 claims description 5
- 239000004455 soybean meal Substances 0.000 claims description 5
- 244000131522 Citrus pyriformis Species 0.000 claims description 4
- 238000002156 mixing Methods 0.000 claims description 4
- 230000008569 process Effects 0.000 claims description 4
- 108091005508 Acid proteases Proteins 0.000 claims description 3
- 235000005979 Citrus limon Nutrition 0.000 claims description 3
- 101000693530 Staphylococcus aureus Staphylokinase Proteins 0.000 claims description 3
- 239000003513 alkali Substances 0.000 claims description 3
- 239000000320 mechanical mixture Substances 0.000 claims description 3
- 238000004806 packaging method and process Methods 0.000 claims description 3
- 238000004321 preservation Methods 0.000 claims description 3
- 239000011347 resin Substances 0.000 claims description 3
- 229920005989 resin Polymers 0.000 claims description 3
- 238000000926 separation method Methods 0.000 claims description 3
- 239000011780 sodium chloride Substances 0.000 claims description 3
- 238000001291 vacuum drying Methods 0.000 claims description 3
- 238000010792 warming Methods 0.000 claims description 3
- OBMZMSLWNNWEJA-XNCRXQDQSA-N C1=CC=2C(C[C@@H]3NC(=O)[C@@H](NC(=O)[C@H](NC(=O)N(CC#CCN(CCCC[C@H](NC(=O)[C@@H](CC4=CC=CC=C4)NC3=O)C(=O)N)CC=C)NC(=O)[C@@H](N)C)CC3=CNC4=C3C=CC=C4)C)=CNC=2C=C1 Chemical compound C1=CC=2C(C[C@@H]3NC(=O)[C@@H](NC(=O)[C@H](NC(=O)N(CC#CCN(CCCC[C@H](NC(=O)[C@@H](CC4=CC=CC=C4)NC3=O)C(=O)N)CC=C)NC(=O)[C@@H](N)C)CC3=CNC4=C3C=CC=C4)C)=CNC=2C=C1 OBMZMSLWNNWEJA-XNCRXQDQSA-N 0.000 claims description 2
- 101710176384 Peptide 1 Proteins 0.000 claims description 2
- 102000004142 Trypsin Human genes 0.000 claims description 2
- 108090000631 Trypsin Proteins 0.000 claims description 2
- 230000029087 digestion Effects 0.000 claims description 2
- CSHFHJNMIMPJST-HOTGVXAUSA-N methyl (2s)-2-[[(2s)-2-[[2-[(2-aminoacetyl)amino]acetyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoate Chemical compound NCC(=O)NCC(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)OC)CC1=CC=CC=C1 CSHFHJNMIMPJST-HOTGVXAUSA-N 0.000 claims description 2
- 239000003595 mist Substances 0.000 claims description 2
- 239000012588 trypsin Substances 0.000 claims description 2
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims 6
- 229910052799 carbon Inorganic materials 0.000 claims 1
- 239000000463 material Substances 0.000 claims 1
- 238000010025 steaming Methods 0.000 claims 1
- 230000036039 immunity Effects 0.000 abstract description 4
- 235000016709 nutrition Nutrition 0.000 abstract description 3
- 230000035764 nutrition Effects 0.000 abstract description 3
- 230000007937 eating Effects 0.000 abstract description 2
- 240000007049 Juglans regia Species 0.000 abstract 2
- 230000003712 anti-aging effect Effects 0.000 abstract 1
- 239000000243 solution Substances 0.000 description 30
- 241000699666 Mus <mouse, genus> Species 0.000 description 27
- 102000035195 Peptidases Human genes 0.000 description 13
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- 210000000822 natural killer cell Anatomy 0.000 description 3
- 210000000056 organ Anatomy 0.000 description 3
- 210000003024 peritoneal macrophage Anatomy 0.000 description 3
- 210000003491 skin Anatomy 0.000 description 3
- 230000007306 turnover Effects 0.000 description 3
- 108010006464 Hemolysin Proteins Proteins 0.000 description 2
- 238000010521 absorption reaction Methods 0.000 description 2
- 150000001413 amino acids Chemical class 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 230000000052 comparative effect Effects 0.000 description 2
- 239000003228 hemolysin Substances 0.000 description 2
- 238000012545 processing Methods 0.000 description 2
- 210000002966 serum Anatomy 0.000 description 2
- 238000001694 spray drying Methods 0.000 description 2
- 238000005507 spraying Methods 0.000 description 2
- 210000002784 stomach Anatomy 0.000 description 2
- 210000001541 thymus gland Anatomy 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 206010020751 Hypersensitivity Diseases 0.000 description 1
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- 230000009286 beneficial effect Effects 0.000 description 1
- 230000017531 blood circulation Effects 0.000 description 1
- 210000000988 bone and bone Anatomy 0.000 description 1
- 235000009508 confectionery Nutrition 0.000 description 1
- 210000002808 connective tissue Anatomy 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 230000003111 delayed effect Effects 0.000 description 1
- 235000019621 digestibility Nutrition 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000004744 fabric Substances 0.000 description 1
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- 230000036737 immune function Effects 0.000 description 1
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- 210000000952 spleen Anatomy 0.000 description 1
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Classifications
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- 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
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- 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
- A23L33/125—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives containing carbohydrate syrups; containing sugars; containing sugar alcohols; containing starch hydrolysates
-
- 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
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
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- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Mycology (AREA)
- Nutrition Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Wood Science & Technology (AREA)
- General Chemical & Material Sciences (AREA)
- Microbiology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Biotechnology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biochemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Abstract
The invention discloses a kind of collagen polypeptide powder, raw material including following mass fraction: soybean peptide 25-32%, corn peptide 16-20%, wheat peptide 10-13%, collagen peptide 17-22%, ovalbumin peptide 9-11%, walnut peptide 4-6%, sea cucumber peptide 0.5-2%, citric acid 2-3%, malic acid 1.5-2%, stevioside 0.2-0.5%；The collagen peptide is marine fish skin collagen oligopeptide；The soybean peptide, corn peptide, wheat peptide, collagen peptide, ovalbumin peptide, walnut peptide, sea cucumber peptide are all made of enzymatic isolation method acquisition.Polypeptide powder obtained is not only full of nutrition, has the function of strengthen immunity, anti-aging, and eating mouth feel is good.
Description
Technical field
The present invention relates to nutriment processing technique fields, and in particular to a kind of collagen polypeptide powder and preparation method thereof.
Background technique
Collagen polypeptide is to become the water of resolvability by then extracting to collagen chain enzymatic hydrolysis
Collagen is solved, is segment, but saves the three-dimensional active three helical polypeptides structure of tool.Collagen (fiber) is one kind by 3
Peptide chain twists into spiral fibrous polymer protein, and Filamentous collagen fabric can make skin keep solid and have bullet
Property, it is present in the positions such as human skin, bone, tooth, tendon, and major physiological function is to do the adhesion substance of connective tissue,
Exist in the form of collagenous fibres in vivo.The principal mode of absorption of human body protein not instead of amino acid, in the form of polypeptide
It absorbs.Collagen polypeptide have height digestibility, in addition on a small quantity oral cavity, stomach by protease effect and nearly one
Outside step are decomposed, oral cavity, the stomach for quickly (fast compared with amino acid 70% speed) passing through people into human body are taken orally, small intestine is directly entered,
By small intestinal absorption, blood circulation of human body system, organ and cell tissue are eventually entered into, plays its physiological action and biology rapidly
Function.Collagen polypeptide powder preparation process at present on the market is complicated, and mouthfeel is poor, and absorption of human body effect is poor.
Summary of the invention
To make up the deficiencies in the prior art, the present invention provides a kind of full of nutrition, strengthen immunity collagen polypeptide
Powder and preparation method thereof.
The present invention is achieved through the following technical solutions: a kind of collagen polypeptide powder, be characterized in that including
The raw material of following mass fraction: soybean peptide 25-32%, corn peptide 16-20%, wheat peptide 10-13%, collagen peptide 17-22% are white
Protein peptides 9-11%, walnut peptide 4-6%, sea cucumber peptide 0.5-2%, citric acid 2-3%, malic acid 1.5-2%, stevioside 0.2-0.5%；Institute
Stating collagen peptide is marine fish skin collagen oligopeptide；The soybean peptide, corn peptide, wheat peptide, collagen peptide, albumin
Peptide, walnut peptide, sea cucumber peptide are all made of enzymatic isolation method acquisition.
Preferably, a kind of collagen polypeptide powder of the invention, the raw material including following mass fraction: soybean peptide
30%, corn peptide 19.1%, wheat peptide 11%, collagen Gly-His-Lys 19%, ovalbumin peptide 10%, walnut peptide 5%, sea cucumber peptide 1%, lemon
Acid 2.5%, malic acid 2%, stevioside 0.4%.
A kind of preparation method of collagen polypeptide powder of the invention, comprising the following steps:
(1) respectively by Soybean Meal, the corn dregs of rice, the wheat dregs of rice, ocean fish-skin, egg white, walnut dregs, sea cucumber leftover bits and pieces by pre- place
It carries out digesting to isolate and purify after reason respectively obtaining soybean peptide, corn peptide, wheat peptide, collagen peptide, ovalbumin peptide, walnut peptide,
Sea cucumber peptide；
(2) by soybean peptide obtained, corn peptide, wheat peptide, collagen peptide, ovalbumin peptide, walnut peptide, sea cucumber peptide and lemon
Acid, malic acid, stevioside mechanical mixture are uniformly spray-dried to obtain powder afterwards, and powder carries out subpackage packaging after crossing 50-100 mesh.
Preferably, the soybean peptide, corn peptide, wheat peptide are all made of following methods and are made: by Soybean Meal, corn
The dregs of rice, the wheat dregs of rice are mixed with water according to weight ratio 1:(6-10), and alkali protease is added and trypsin digestion, hydrolysis temperature are
45-65 DEG C, enzymolysis liquid pH value is 7-9, is filtered to remove impurity in enzymolysis liquid after keeping the temperature 2-4h, and filtrate carries out secondary enzymolysis again,
Enzymatic hydrolysis condition is identical as first time, and into secondary enzymatic solution plus acid for adjusting pH value is to 4-6, and centrifuge separation obtains supernatant；By supernatant
Liquid carries out decoloration taste removal by macroreticular resin according to the speed of 2-3mL/min, spray drying, can be obtained soybean peptide, corn peptide,
The powder of wheat peptide.
Preferably, the collagen peptide is obtained using following methods: after ocean fish-skin is cleaned and dried, being impregnated
In the sodium hydroxide solution of 0.05mol/L, ocean fish-skin is isolated after soak at room temperature 2-4h, wash with distilled water completely；It will
Processed ocean fish-skin is put into its 8-10 times distilled water of weight, and the neutral protease enzymolysis 4-8h that 1-1.5% is added obtains collagen
Protein solution, hydrolysis temperature are 25-45 DEG C, and enzymatic hydrolysis pressure is 0.01-0.03MPa；Into the collagen solution that enzymatic hydrolysis obtains
The activated carbon adsorption for weighing its 1.5-2.5% is added, at normal temperature, pressure control separates pure after 0.03-0.05MPa, 30-50min
Collagen solution is dissolved, beta-cyclodextrin is added into collagen solution and is coated, is then spray-dried at 40-70 DEG C
Collagen Gly-His-Lys.
Preferably, the ovalbumin peptide is obtained using following methods: after egg white is diluted with water mixing, being adjusted
Section pH value is 7-9, and neutral proteinase is added and flavor protease is digested, and hydrolysis temperature is 45-65 DEG C, and enzymolysis liquid keeps the temperature 3-
The impurity being filtered to remove in enzymolysis liquid after 5h, into enzymolysis liquid plus acid for adjusting pH is 3-5, and acid protease is then added and carries out two
Secondary enzymatic hydrolysis heats up enzyme deactivation after digesting 0.5-1h, and cooled and filtered obtains clarified solution, is spray-dried, ovalbumin peptide powder can be obtained.
Preferably, the walnut peptide is obtained using following methods: it will be crushed after walnut dregs vacuum drying, add water,
PH value 5-6 is adjusted, is warming up to 50-60 DEG C, compound protease is added and flavor protease is digested, compound protease and flavor
Protease mass ratio 1:1 digests 3h, and per half an hour adjusts a pH in enzymolysis process, and pH value is made to maintain 5-6, enzymatic hydrolysis knot
Enzyme deactivation after beam filters to obtain clarified solution, is spray-dried after filtrate concentration, walnut peptide powder can be obtained.
Preferably, the sea cucumber peptide is obtained using following methods: after sea cucumber leftover bits and pieces is cleaned and dried, being immersed in
In the sodium chloride solution of 0.1mol/L, sea cucumber leftover bits and pieces is isolated after soak at room temperature 2-3h, wash with distilled water completely；It will processing
The sea cucumber leftover bits and pieces crossed is put into its 8-10 times distilled water of weight, and the neutral protease enzymolysis 4-8h that 1-1.5% is added obtains collagen egg
White solution, hydrolysis temperature are 25-45 DEG C, and enzymatic hydrolysis pressure is 0.01-0.03MPa；Add into the collagen solution that enzymatic hydrolysis obtains
Enter to weigh the activated carbon adsorption of its 1.5-2.5%, at normal temperature, pressure control isolates and purifies after 0.03-0.05MPa, 30-50min
Collagen solution out is added beta-cyclodextrin into collagen solution and is coated, is then spray-dried at 40-70 DEG C extra large
Join peptide powder.
The beneficial effects of the present invention are: different protein peptides are made by enzymolysis process in the present invention, preparation process is simple, energy
Wherein foreign protein and the miscellaneous taste of various fishy smell are sufficiently removed, polypeptide powder obtained is not only full of nutrition, the work with strengthen immunity
With, and eating mouth feel is good.
Detailed description of the invention
Fig. 1 is the relational graph of influence of each dosage group of the present invention to mice organs weight ratio；
Fig. 2 is the relational graph of influence of each group of the present invention to mouse thymus weight ratio；
Fig. 3 is the relational graph of influence of each group of the present invention to mouse delayed allergy (DTH)；
Fig. 4 is the relational graph of influence of each group of the present invention to the ConA mouse lymphocyte transformation experiment induced；
Fig. 5 is the relational graph of influence of each group of the present invention to mouse antibodies cellulation number；
Fig. 6 is the relational graph of influence of each group of the present invention to mice serum hemolysin；
Fig. 7 is relational graph of each group of the present invention to the influence of mouse monokaryon-macrophage function；
Fig. 8 is the relational graph of influence of each group of the present invention to Turnover of Mouse Peritoneal Macrophages chicken red blood cell phagocytic rate function；
Fig. 9 is each group of the present invention on the active influence of NK cells in mice.
Specific embodiment
The present invention will be further described in detail with reference to the specific embodiments, to help those skilled in the art
There is more complete, accurate and deep understanding to inventive concept of the invention, technical solution, protection scope of the present invention includes but not
It is limited to following embodiment, the details of any pair of technical solution of the present invention under the premise of without departing from spirit and scope
It is fallen within the protection scope of the present invention with the modification that form is made.
Embodiment 1
The collagen polypeptide powder of the present embodiment, including following raw material: soybean peptide 25g, corn peptide 16g, wheat peptide 10g, collagen
Protein peptides 22g, ovalbumin peptide 11g, walnut peptide 4g, sea cucumber peptide 2g, citric acid 3g, malic acid 1.5g, stevioside 0.2g.
The preparation method of the collagen polypeptide powder of the present embodiment, comprising the following steps:
(1) Soybean Meal, the corn dregs of rice, the wheat dregs of rice are mixed with water according to weight ratio 1:8, alkali protease and trypsase enzyme is added
Solution, hydrolysis temperature are 55 DEG C, and enzymolysis liquid pH value is 7, and the impurity being filtered to remove in enzymolysis liquid after heat preservation 3h, filtrate carries out secondary again
Enzymatic hydrolysis, enzymatic hydrolysis condition is identical as first time, and into secondary enzymatic solution plus acid for adjusting pH value is to 5, and centrifuge separation obtains supernatant；It will
Supernatant carries out decoloration taste removal by macroreticular resin according to the speed of 3ml/min, and soybean peptide, corn can be obtained in spray drying
The powder of peptide, wheat peptide.
(2) it after being cleaned and dried ocean fish-skin, is immersed in the sodium hydroxide solution of 0.05mol/L, after soak at room temperature 2h
Ocean fish-skin is isolated, wash with distilled water completely；Processed ocean fish-skin is put into its 10 times distilled water of weight, is added
1.5% neutral protease enzymolysis 4h obtains collagen solution, and hydrolysis temperature is 40 DEG C, and enzymatic hydrolysis pressure is 0.02MPa；To enzymatic hydrolysis
Its 1.5% activated carbon adsorption of weight is added in obtained collagen solution, at normal temperature, pressure is controlled in 0.03MPa, 40min
After isolate and purify out collagen solution, into collagen solution be added beta-cyclodextrin coated, then 40-70 DEG C spray
Mist it is dry collagen Gly-His-Lys.
(3) after egg white being diluted with water mixing, adjusting pH value is 7, be added neutral proteinase and flavor protease into
Row enzymatic hydrolysis, hydrolysis temperature are 65 DEG C, and the impurity being filtered to remove in enzymolysis liquid after enzymolysis liquid heat preservation 5h, into enzymolysis liquid, acid adding is adjusted
PH is 3, and acid protease is then added and carries out secondary enzymolysis, heat up enzyme deactivation after enzymatic hydrolysis 1h, and cooled and filtered obtains clarified solution, spraying
It is dry, ovalbumin peptide powder can be obtained.
(4) it will be crushed after walnut dregs vacuum drying, add water, adjust pH value 5.5, be warming up to 55 DEG C, compound protease is added
It is digested with flavor protease, compound protease and flavor protease mass ratio 1:1, enzymatic hydrolysis 3h, every half in enzymolysis process
Hour adjusts a pH, and pH value is made to maintain 5.5, and enzyme deactivation after enzymatic hydrolysis is filtered to obtain clarified solution, done by spraying after filtrate concentration
It is dry, walnut peptide powder can be obtained.
(5) it after being cleaned and dried sea cucumber leftover bits and pieces, is immersed in the sodium chloride solution of 0.1mol/L, divides after soak at room temperature 2h
Sea cucumber leftover bits and pieces is separated out, wash with distilled water completely；Processed sea cucumber leftover bits and pieces is put into its 10 times distilled water of weight, is added
The neutral protease enzymolysis 5h for entering 1.5% obtains collagen solution, and hydrolysis temperature is 30 DEG C, and enzymatic hydrolysis pressure is 0.02MPa；To enzyme
Its 2.5% activated carbon adsorption of weight is added in the collagen solution that solution obtains, at normal temperature, pressure is controlled in 0.05MPa,
Collagen solution is isolated and purified out after 50min, and beta-cyclodextrin is added into collagen solution and is coated, then at 50 DEG C
It is spray-dried to obtain sea cucumber peptide powder.
(6) by soybean peptide obtained, corn peptide, wheat peptide, collagen peptide, ovalbumin peptide, walnut peptide, sea cucumber peptide and lemon
Lemon acid, malic acid, stevioside mechanical mixture are uniformly spray-dried to obtain powder afterwards, and powder carries out subpackage packaging after sieving with 100 mesh sieve, often
Wrap 5g.
Embodiment 2
A kind of collagen polypeptide powder, the raw material including following mass fraction: soybean peptide 300g, corn peptide 191g, wheat peptide
110g, collagen Gly-His-Lys 190g, ovalbumin peptide 100g, walnut peptide 50g, sea cucumber peptide 10g, citric acid 25g, malic acid 20g, sweet tea
Synanthrin 4g.
The collagen polypeptide powder, preparation method thereof of the present embodiment is the same as embodiment 1.
Embodiment 3
A kind of collagen polypeptide powder, the raw material including following mass fraction: soybean peptide 32g, corn peptide 20g, wheat peptide 13g,
Collagen peptide 17g, ovalbumin peptide 9g, walnut peptide 6g, sea cucumber peptide 1g, citric acid 2g, malic acid 2g, stevioside 0.3g.
The collagen polypeptide powder, preparation method thereof of the present embodiment is the same as embodiment 1.
The zoopery of strengthen immunity of the present invention is as follows:
1. influence of each dosage group to mice organs weight ratio
As seen from Figure 1, orally administration mouse various dose sample 30 days meets variance after initial data progress variance is examined together
Neat requirement carries out statistical analysis with one-way analysis of variance method.It can be concluded that water control group and 3 dosage groups totally four
The results of analysis of variance of a group of spleen weight ratio shows, no significant difference (p > 0.05) between each group mean.
From Figure 2 it can be seen that orally administration mouse various dose sample 30 days, after initial data progress variance is examined together, meet
The neat requirement of variance carries out statistical analysis with one-way analysis of variance method.It can be concluded that water control group and 3 dosage groups
The results of analysis of variance of the thymus gland weight ratio of totally four groups is shown, no significant difference (p > 0.05) between each group mean.
2. the influence pair mouse cell immune function
As seen from Figure 3, orally administration mouse various dose sample 30 days meets variance after initial data progress variance is examined together
Neat requirement carries out statistical analysis with one-way analysis of variance method.It can be concluded that water control group and 3 dosage groups totally four
The results of analysis of variance of a group of mouse swelling degree of the paw shows, no significant difference (p > 0.05) between each group mean.
From fig. 4, it can be seen that orally administration mouse various dose sample 30 days, after initial data progress variance is examined together, meet
The neat requirement of variance carries out statistical analysis with one-way analysis of variance method.It can be concluded that water control group and 3 dosage groups
The results of analysis of variance of the mouse lymphocyte proliferative capacity of totally four groups is shown, difference has middle and high dosage compared with the control group
Conspicuousness (p < 0.05) has the ability for the mouse lymphocyte conversion for increasing ConA induction.
3. the influence of pair mouse humoral immune
3.1 influence mouse antibodies cellulation number
As seen from Figure 5, orally administration mouse various dose sample 30 days meets variance after initial data progress variance is examined together
Neat requirement carries out statistical analysis with one-way analysis of variance method.It can be concluded that water control group and 3 dosage groups totally four
The results of analysis of variance of a group of antibody-producting cell number shows that difference has conspicuousness (p < 0.05) between each group mean.With more
The comparative approach two-by-two of mean carries out statistical analysis between a experimental group and a control group, and antibody-producting cell number is in water pair
Have compared between each dosage group according to group significant difference (p < 0.05), it is believed that this time laboratory sample has increase mouse
The ability of antibody-producting cell number.
The influence of 3.2 pairs of mice serum hemolysins
As seen from Figure 6, orally administration mouse various dose sample 30 days meets variance after initial data progress variance is examined together
Neat requirement carries out statistical analysis with one-way analysis of variance method.It can be concluded that water control group and 3 dosage groups totally four
The results of analysis of variance of a group of mouse antibodies product shows, more equal conspicuousness (p > 0.05) difference between each group mean.
3.3 pairs of mouse monokaryon-macrophage function influences
As seen from Figure 7, orally administration mouse various dose sample 30 days meets variance after initial data progress variance is examined together
Neat requirement carries out statistical analysis with one-way analysis of variance method.It can be concluded that water control group and 3 dosage groups totally four
The results of analysis of variance of a group of mouse phagocytic index shows, no significant difference (p > 0.05) between each group mean.
The influence of 3.4 pairs of Turnover of Mouse Peritoneal Macrophages chicken red blood cell phagocytic rate functions
As seen from Figure 8, orally administration mouse various dose sample 30 days, the square root arcsin transformation value after phagocytic rate conversion gulp down
It bites index and is all satisfied homogeneity of variance requirement, carry out statistical analysis with one-way analysis of variance.It can be concluded that phagocytic rate conversion value
There is conspicuousness (p>0.05) difference between each group mean, there is conspicuousness (p<0.05) difference between phagocytic index each group mean, uses
The comparative approach two-by-two of mean carries out statistical analysis between multiple experimental groups and a control group, and phagocytic index is in water control group
There was no significant difference compared between low dose group (p > 0.05), has significantly in water control group and middle and high dosage comparison among groups
Sex differernce (p < 0.05) has and promotes Turnover of Mouse Peritoneal Macrophages to the phagocytic activity of chicken red blood cell.
4. on the active influence of NK cells in mice
As seen from Figure 9, orally administration mouse various dose sample 30 days meets variance after initial data progress variance is examined together
Neat requirement carries out statistical analysis with one-way analysis of variance method.It can be concluded that water control group and 3 dosage groups totally four
The results of analysis of variance of a group of NK cells in mice activity conversion value shows, no significant difference between each group mean (p >
0.05).
Claims (8)
1. a kind of collagen polypeptide powder, it is characterised in that: the raw material including following mass fraction: soybean peptide 25-32%, corn
Peptide 16-20%, wheat peptide 10-13%, collagen peptide 17-22%, ovalbumin peptide 9-11%, walnut peptide 4-6%, sea cucumber peptide 0.5-2%,
Citric acid 2-3%, malic acid 1.5-2%, stevioside 0.2-0.5%；The collagen peptide is marine fish skin collagen oligopeptide；Institute
It states soybean peptide, corn peptide, wheat peptide, collagen peptide, ovalbumin peptide, walnut peptide, sea cucumber peptide and is all made of enzymatic isolation method acquisition.
2. a kind of collagen polypeptide powder according to claim 1, it is characterised in that: the original including following mass fraction
Material: soybean peptide 30%, corn peptide 19.1%, wheat peptide 11%, collagen Gly-His-Lys 19%, ovalbumin peptide 10%, walnut peptide 5%, sea cucumber
Peptide 1%, citric acid 2.5%, malic acid 2%, stevioside 0.4%.
3. a kind of preparation method of collagen polypeptide powder according to claim 1 or 2, it is characterised in that: including following
Step:
(1) respectively by Soybean Meal, the corn dregs of rice, the wheat dregs of rice, ocean fish-skin, egg white, walnut dregs, sea cucumber leftover bits and pieces by pre- place
It carries out digesting to isolate and purify after reason respectively obtaining soybean peptide, corn peptide, wheat peptide, collagen peptide, ovalbumin peptide, walnut peptide,
Sea cucumber peptide；
(2) by soybean peptide obtained, corn peptide, wheat peptide, collagen peptide, ovalbumin peptide, walnut peptide, sea cucumber peptide and lemon
Acid, malic acid, stevioside mechanical mixture are uniformly spray-dried to obtain powder afterwards, and powder carries out subpackage packaging after crossing 50-100 mesh.
4. a kind of preparation method of collagen polypeptide powder according to claim 3, it is characterised in that: the soybean peptide,
Corn peptide, wheat peptide are all made of following methods and are made: by Soybean Meal, the corn dregs of rice, the wheat dregs of rice and water according to weight ratio 1:(6-10)
Alkali protease and trypsin digestion is added in mixing, and hydrolysis temperature is 45-65 DEG C, and enzymolysis liquid pH value is 7-9, keeps the temperature 2-4h
The impurity being filtered to remove in enzymolysis liquid afterwards, filtrate carry out secondary enzymolysis again, and enzymatic hydrolysis condition is identical as first time, to secondary enzymatic solution
In plus acid for adjusting pH value to 4-6, centrifuge separation obtains supernatant；Supernatant is passed through into macroreticular resin according to the speed of 2-3mL/min
Carry out decoloration taste removal, be spray-dried, can be obtained soybean peptide, corn peptide, wheat peptide powder.
5. a kind of preparation method of collagen polypeptide powder according to claim 3, it is characterised in that: the collagen
Peptide is obtained using following methods: after ocean fish-skin is cleaned and dried, being immersed in the sodium hydroxide solution of 0.05mol/L, room temperature
Ocean fish-skin is isolated after impregnating 2-4h, wash with distilled water completely；Processed ocean fish-skin is put into its 8-10 times of weight
In distilled water, the neutral protease enzymolysis 4-8h that 1-1.5% is added obtains collagen solution, and hydrolysis temperature is 25-45 DEG C, enzymatic hydrolysis
Pressure is 0.01-0.03MPa；The activated carbon adsorption of its 1.5-2.5% of weight is added into the collagen solution that enzymatic hydrolysis obtains,
Under room temperature, pressure control isolates and purifies out collagen solution after 0.03-0.05MPa, 30-50min, to collagen solution
Middle addition beta-cyclodextrin is coated, and collagen Gly-His-Lys are then spray-dried to obtain at 40-70 DEG C.
6. a kind of preparation method of collagen polypeptide powder according to claim 3, it is characterised in that: the ovalbumin peptide
Obtained using following methods: after egg white is diluted with water mixing, adjusting pH value is 7-9, and neutral proteinase and flavor is added
Protease is digested, and hydrolysis temperature is 45-65 DEG C, the impurity being filtered to remove in enzymolysis liquid after enzymolysis liquid heat preservation 3-5h, to enzyme
In solution liquid plus acid for adjusting pH is 3-5, and acid protease is then added and carries out secondary enzymolysis, heat up enzyme deactivation after enzymatic hydrolysis 0.5-1h, cold
But clarified solution is filtered to obtain afterwards, is spray-dried, ovalbumin peptide powder can be obtained.
7. a kind of preparation method of collagen polypeptide powder according to claim 3, it is characterised in that: the walnut peptide is adopted
It obtains: will be crushed after walnut dregs vacuum drying using the following method, add water, adjust pH value 5-6, be warming up to 50-60 DEG C, be added compound
Protease and flavor protease are digested, compound protease and flavor protease mass ratio 1:1, enzymatic hydrolysis 3h, in enzymolysis process
Per half an hour adjusts a pH, and pH value is made to maintain 5-6, and enzyme deactivation after enzymatic hydrolysis is filtered to obtain clarified solution, sprayed after filtrate concentration
Mist is dry, and walnut peptide powder can be obtained.
8. a kind of preparation method of collagen polypeptide powder according to claim 3, it is characterised in that: the sea cucumber peptide is adopted
It obtains: after sea cucumber leftover bits and pieces is cleaned and dried, being immersed in the sodium chloride solution of 0.1moL/L, soak at room temperature 2- using the following method
Sea cucumber leftover bits and pieces is isolated after 3h, wash with distilled water completely；Processed sea cucumber leftover bits and pieces is put into its 8-10 times steaming of weight
In distilled water, the neutral protease enzymolysis 4-8h that 1-1.5% is added obtains collagen solution, and hydrolysis temperature is 25-45 DEG C, enzymatic hydrolysis pressure
Power is 0.01-0.03MPa；The activated carbon adsorption of its 1.5-2.5% of weight is added into the collagen solution that enzymatic hydrolysis obtains, normal
Under temperature, pressure control isolates and purifies out collagen solution after 0.03-0.05MPa, 30-50min, into collagen solution
Beta-cyclodextrin is added to be coated, sea cucumber peptide powder is then spray-dried to obtain at 40-70 DEG C.
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