CN106916869B - Potato active peptide and preparation method thereof - Google Patents
Potato active peptide and preparation method thereof Download PDFInfo
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- CN106916869B CN106916869B CN201710258298.XA CN201710258298A CN106916869B CN 106916869 B CN106916869 B CN 106916869B CN 201710258298 A CN201710258298 A CN 201710258298A CN 106916869 B CN106916869 B CN 106916869B
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- 244000061456 Solanum tuberosum Species 0.000 title claims abstract description 69
- 235000002595 Solanum tuberosum Nutrition 0.000 title claims abstract description 68
- 238000002360 preparation method Methods 0.000 title claims abstract description 32
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- 108090000623 proteins and genes Proteins 0.000 claims abstract description 90
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- 238000000265 homogenisation Methods 0.000 claims abstract description 18
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- 238000001035 drying Methods 0.000 claims abstract description 14
- 238000000034 method Methods 0.000 claims abstract description 14
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- 244000017020 Ipomoea batatas Species 0.000 claims description 81
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- 108091005658 Basic proteases Proteins 0.000 claims description 22
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- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 claims description 12
- 238000004140 cleaning Methods 0.000 claims description 12
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- TUJKJAMUKRIRHC-UHFFFAOYSA-N hydroxyl Chemical compound [OH] TUJKJAMUKRIRHC-UHFFFAOYSA-N 0.000 description 7
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- GVJHHUAWPYXKBD-UHFFFAOYSA-N (±)-α-Tocopherol Chemical compound OC1=C(C)C(C)=C2OC(CCCC(C)CCCC(C)CCCC(C)C)(C)CCC2=C1C GVJHHUAWPYXKBD-UHFFFAOYSA-N 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
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- LXEKPEMOWBOYRF-QDBORUFSSA-N AAPH Chemical compound Cl.Cl.NC(=N)C(C)(C)\N=N\C(C)(C)C(N)=N LXEKPEMOWBOYRF-QDBORUFSSA-N 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
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- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
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- 229910019142 PO4 Inorganic materials 0.000 description 2
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 2
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- WIGCFUFOHFEKBI-UHFFFAOYSA-N gamma-tocopherol Natural products CC(C)CCCC(C)CCCC(C)CCCC1CCC2C(C)C(O)C(C)C(C)C2O1 WIGCFUFOHFEKBI-UHFFFAOYSA-N 0.000 description 2
- 230000036541 health Effects 0.000 description 2
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- 238000009931 pascalization Methods 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 2
- 239000010452 phosphate Substances 0.000 description 2
- 239000008055 phosphate buffer solution Substances 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 235000019165 vitamin E Nutrition 0.000 description 2
- 229940046009 vitamin E Drugs 0.000 description 2
- 239000011709 vitamin E Substances 0.000 description 2
- 239000002699 waste material Substances 0.000 description 2
- 108010039627 Aprotinin Proteins 0.000 description 1
- 102000018832 Cytochromes Human genes 0.000 description 1
- 108010052832 Cytochromes Proteins 0.000 description 1
- 108010082495 Dietary Plant Proteins Proteins 0.000 description 1
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 229910021577 Iron(II) chloride Inorganic materials 0.000 description 1
- 240000007594 Oryza sativa Species 0.000 description 1
- 235000007164 Oryza sativa Nutrition 0.000 description 1
- 239000012505 Superdex™ Substances 0.000 description 1
- 235000021307 Triticum Nutrition 0.000 description 1
- 244000098338 Triticum aestivum Species 0.000 description 1
- 229930003779 Vitamin B12 Natural products 0.000 description 1
- 240000008042 Zea mays Species 0.000 description 1
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 1
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 1
- XNHPXELLWREZKM-UHFFFAOYSA-N [Na].C=1C=CC=CC=1S(=O)(=O)OC1=CC=CC=C1 Chemical compound [Na].C=1C=CC=CC=1S(=O)(=O)OC1=CC=CC=C1 XNHPXELLWREZKM-UHFFFAOYSA-N 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 229960000583 acetic acid Drugs 0.000 description 1
- 229960004405 aprotinin Drugs 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
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- FDJOLVPMNUYSCM-WZHZPDAFSA-L cobalt(3+);[(2r,3s,4r,5s)-5-(5,6-dimethylbenzimidazol-1-yl)-4-hydroxy-2-(hydroxymethyl)oxolan-3-yl] [(2r)-1-[3-[(1r,2r,3r,4z,7s,9z,12s,13s,14z,17s,18s,19r)-2,13,18-tris(2-amino-2-oxoethyl)-7,12,17-tris(3-amino-3-oxopropyl)-3,5,8,8,13,15,18,19-octamethyl-2 Chemical compound [Co+3].N#[C-].N([C@@H]([C@]1(C)[N-]\C([C@H]([C@@]1(CC(N)=O)C)CCC(N)=O)=C(\C)/C1=N/C([C@H]([C@@]1(CC(N)=O)C)CCC(N)=O)=C\C1=N\C([C@H](C1(C)C)CCC(N)=O)=C/1C)[C@@H]2CC(N)=O)=C\1[C@]2(C)CCC(=O)NC[C@@H](C)OP([O-])(=O)O[C@H]1[C@@H](O)[C@@H](N2C3=CC(C)=C(C)C=C3N=C2)O[C@@H]1CO FDJOLVPMNUYSCM-WZHZPDAFSA-L 0.000 description 1
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- 235000005822 corn Nutrition 0.000 description 1
- 230000009849 deactivation Effects 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
- 239000003480 eluent Substances 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
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- GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 1
- 229940020947 fluorescein sodium Drugs 0.000 description 1
- 238000009920 food preservation Methods 0.000 description 1
- 239000012362 glacial acetic acid Substances 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 229910052603 melanterite Inorganic materials 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 229940054441 o-phthalaldehyde Drugs 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 239000002953 phosphate buffered saline Substances 0.000 description 1
- ZWLUXSQADUDCSB-UHFFFAOYSA-N phthalaldehyde Chemical compound O=CC1=CC=CC=C1C=O ZWLUXSQADUDCSB-UHFFFAOYSA-N 0.000 description 1
- 230000001766 physiological effect Effects 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 239000012460 protein solution Substances 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 235000009566 rice Nutrition 0.000 description 1
- 230000002000 scavenging effect Effects 0.000 description 1
- 239000001509 sodium citrate Substances 0.000 description 1
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 1
- 230000002195 synergetic effect Effects 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 235000019587 texture Nutrition 0.000 description 1
- 229910021642 ultra pure water Inorganic materials 0.000 description 1
- 239000012498 ultrapure water Substances 0.000 description 1
- 235000013311 vegetables Nutrition 0.000 description 1
- 235000019163 vitamin B12 Nutrition 0.000 description 1
- 239000011715 vitamin B12 Substances 0.000 description 1
Classifications
-
- 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
- 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
- A61Q19/08—Anti-ageing preparations
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
- C07K1/145—Extraction; Separation; Purification by extraction or solubilisation
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Veterinary Medicine (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Engineering & Computer Science (AREA)
- Genetics & Genomics (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Epidemiology (AREA)
- Birds (AREA)
- Dermatology (AREA)
- General Chemical & Material Sciences (AREA)
- General Engineering & Computer Science (AREA)
- Gerontology & Geriatric Medicine (AREA)
- Analytical Chemistry (AREA)
- Biophysics (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Cosmetics (AREA)
- Peptides Or Proteins (AREA)
Abstract
本发明提供一种薯类活性肽及其制备方法，包括如下步骤：(1)采用超声波协同高压均质对薯类蛋白进行处理；(2)高静压下酶解薯类蛋白，再经灭酶、离心、除盐、干燥后，即得薯类活性肽。利用本发明所生产的活性肽，能够有效清除自由基、螯合金属离子，因此具有延缓食品系统氧化、提高食品稳定性、延缓机体衰老及减少氧化损伤等特点。本发明的薯类蛋白活性肽可应用于制备功能食品，能够提高薯类加工产品附加值，且在食品及化妆品等领域中具有广阔的应用前景。本发明提供的制备工艺简单，易于产业化生产。The invention provides a potato active peptide and a preparation method thereof, comprising the following steps: (1) using ultrasonic waves to synergize high pressure homogenization to process the potato protein; (2) enzymatically hydrolyzing the potato protein under high static pressure, and then sterilizing the potato protein. After enzyme, centrifugation, desalination and drying, the potato active peptide is obtained. The active peptide produced by the invention can effectively scavenge free radicals and chelate metal ions, so it has the characteristics of delaying the oxidation of food system, improving food stability, delaying body aging and reducing oxidative damage. The potato protein active peptide of the invention can be applied to prepare functional food, can increase the added value of potato processed products, and has broad application prospects in the fields of food and cosmetics. The preparation process provided by the invention is simple and easy for industrial production.
Description
Technical Field
The invention relates to the technical field of food processing, in particular to a potato active peptide and a preparation method thereof.
Background
China is a big country for planting and producing potatoes, and annual output is at the top of the world. Potatoes are the fourth major food crop listed behind rice, corn, wheat. In China industry, potatoes are mainly used for producing starch, and a large amount of potato pulp is generated in the process. Taking sweet potatoes as an example, according to incomplete statistics, about 900 million tons of sweet potatoes are used for processing starch in China every year, so that about 2000 million tons of sweet potato pulp can be generated, wherein about 12 million tons of sweet potato protein is contained, and the annual demand of more than 430 million people on protein can be met according to the consumption of 75 grams of protein in China per capita, however, the sweet potato pulp is often directly discharged as waste liquid, so that serious environmental pollution and huge resource waste are caused. Compared with most other vegetable proteins, the potato protein has higher content of essential amino acids, has acceptable nutritional value and is a potential source of active peptides of vegetable origin.
High hydrostatic pressure processing techniques have experienced tremendous growth over the past two decades and the industrial application in the food industry, such as food preservation and creation of new foods, textures and flavors, etc., has become a reality. When the high hydrostatic pressure technology is applied to a protein solution, a protein chain can be stretched, so that more enzyme cutting sites are exposed, the enzymolysis reaction is facilitated, and some new functional peptides with special physiological activity can be generated. The food-derived bioactive peptides have the characteristics of low molecular weight, high activity, easy absorption and the like, and are considered to be safe and healthy. More importantly, the food-derived bioactive peptides also exhibit good nutritional and functional properties.
Therefore, the development of the potato active peptide and the establishment of the preparation method thereof have important significance for promoting the sustainable development of potato processing industry in China, ensuring food safety in China and improving the dietary nutrition of residents.
Disclosure of Invention
The invention aims to provide a potato active peptide and a preparation method thereof.
In order to realize the purpose of the invention, the potato active peptide and the preparation method thereof comprise the following steps:
(1) processing the potato protein by adopting an ultrasonic wave synergistic high-pressure homogenization method;
(2) carrying out enzymolysis on potato protein under high static pressure, and then carrying out enzyme deactivation, centrifugation, desalting and drying to obtain the potato active peptide.
In the preparation method of the potato active peptide, potatoes, sweet potatoes and cassava are used as potatoes, sweet potatoes and cassava, and preferably the potatoes and the sweet potatoes are used as potatoes. The preparation method of the potato protein comprises the following steps: the potato protein is prepared by using potatoes as raw materials, cleaning, peeling, cutting into blocks, adding 0.2-0.5% citric acid aqueous solution (with Vc concentration of 0.01-0.1%) according to the material-liquid ratio of 1:1, pulping, filtering to remove residues, centrifuging to remove starch, ultrafiltering, concentrating, and freeze-drying.
In the preparation method of the potato active peptide, the ultrasonic power is 50-400W, preferably 200W; the ultrasonic time is 1-10min, preferably 5 min.
In the preparation method of the active peptide, the high-pressure homogenizing pressure in the step (1) is 10-150MPa, preferably 120 MPa; the high pressure homogenizing time is 0.5-10min, preferably 1 min.
In the step (1), before homogenizing the potato protein, the potato protein is mixed according to the ratio of g: 1 mL: 20-100 in Tris-HCl buffer solution with pH value of 7-9.
In the step (2) of the preparation method of the active peptide, alkaline protease Alcalase is adopted for enzymolysis, and the alkaline protease Alcalase and potato protein are mixed according to the ratio of g: 1 mL: mixing at a ratio of 10-50. Performing enzymolysis at 50-60 deg.C for 30-240min, preferably at 57 deg.C.
In the step (2) of the preparation method of the active peptide, the high static pressure is 600MPa, preferably 300 MPa; the high static pressure pressurizing time is 30-240min, preferably 120 min.
As a preferred embodiment of the present invention, the method for preparing the active peptide of the present invention comprises the following steps:
the potato protein is prepared by the following steps: 1 mL: dissolving the mixture in Tris-HCl buffer solution with the pH value of 7-9 in the proportion of 20-100, treating the potato protein by adopting 50-400W ultrasonic waves for 1-10min, then carrying out high-pressure homogenization treatment on the potato protein under the pressure of 10-150MPa for 0.5-10min, and mixing alkaline protease Alcalase and the potato protein according to the weight ratio of g: 1 mL: 10-50, packaging, performing enzymolysis at 50-60 ℃ for 30-240min under high static pressure of 600MPa at 100-.
The invention also provides the potato active peptide prepared by the method.
It is understood by those skilled in the art that the application of the active peptide of potato obtained by the above method of the present invention in preparing food or cosmetics also falls within the scope of the present invention.
The invention has the following advantages:
1) the active peptide prepared by the invention has high antioxidant activity and low molecular weight, and is easy to be absorbed and utilized by human bodies.
2) The active peptide provided by the invention has rich essential amino acid content and has health care effect;
3) the active peptide provided by the invention overcomes the defects of low activity and poor stability of the existing protein peptide, can be widely applied to the field of food, and is beneficial to improving the dietary nutrition and health of residents.
4) The preparation method of the active peptide provided by the invention is simple to operate and easy for industrial production.
Detailed Description
The following examples are intended to illustrate the invention but are not intended to limit the scope of the invention. Unless otherwise specified, the technical means used in the examples are conventional means well known to those skilled in the art, and the raw materials used are commercially available products.
The percent in the present invention means mass percent unless otherwise specified; but the percent of the solution, unless otherwise specified, refers to the grams of solute contained in 100mL of the solution.
EXAMPLE 1 preparation of a Potato active peptide (1)
Cleaning sweet potato, peeling, cutting into blocks, adding 0.2% citric acid aqueous solution (containing Vc concentration of 0.1%) according to the material-liquid ratio of 1:1, pulping, filtering to remove residue, centrifuging to remove starch, ultrafiltering, concentrating, and lyophilizing to obtain sweet potato protein. Mixing sweet potato protein according to the weight ratio of g: 1 mL: 30 in the ratio of the alkaline protease Alcalase and the sweet potato protein are dissolved in Tris-HCl buffer solution with the pH value of 8.3, the sweet potato protein is treated by 200W ultrasonic wave for 5min, then the sweet potato protein is treated by high-pressure homogenization under the pressure of 120MPa for 1min, and the alkaline protease Alcalase and the sweet potato protein are mixed according to the weight ratio of g: 1 mL: 25, packaging, performing enzymolysis at a high static pressure of 300MPa at 57 ℃ for 120min, taking out, deactivating enzyme at 100 ℃ for 10min, centrifuging at 10000g for 60min, desalting, and drying to obtain the sweet potato peptide.
Example 2 preparation of a Potato active peptide (2)
Cleaning sweet potato, peeling, cutting into blocks, adding 0.3% citric acid aqueous solution (containing Vc concentration of 0.05%) according to a material-liquid ratio of 1:1, pulping, filtering to remove residues, centrifuging to remove starch, ultrafiltering, concentrating, and lyophilizing to obtain sweet potato protein. Mixing sweet potato protein according to the weight ratio of g: 1 mL: 25 in the ratio of the alkaline protease Alcalase to the sweet potato protein, dissolving the mixture in Tris-HCl buffer solution with the pH value of 8.0, treating the sweet potato protein by adopting 400W ultrasonic waves for 3min, then carrying out high-pressure homogenization treatment on the sweet potato protein under the pressure of 100MPa for 2min, and mixing the alkaline protease Alcalase and the sweet potato protein according to the weight ratio of g: 1 mL: 25, packaging, performing enzymolysis at a high static pressure of 300MPa at 57 ℃ for 120min, taking out, deactivating enzyme at 100 ℃ for 10min, centrifuging at 10000g for 60min, desalting, and drying to obtain the sweet potato peptide.
Example 3 preparation of a Potato active peptide (3)
Cleaning sweet potato, peeling, cutting into blocks, adding 0.25% citric acid aqueous solution (containing Vc concentration of 0.02%) according to a material-liquid ratio of 1:1, pulping, filtering to remove residues, centrifuging to remove starch, ultrafiltering, concentrating, and lyophilizing to obtain sweet potato protein. Mixing sweet potato protein according to the weight ratio of g: 1 mL: 35 in a ratio of 8.2, treating the sweet potato protein by adopting 100W ultrasonic waves for 8min, then carrying out high-pressure homogenization treatment on the sweet potato protein for 0.5min under 150MPa, and mixing alkaline protease Alcalase and the sweet potato protein according to the weight ratio of g: 1 mL: 25, packaging, performing enzymolysis at a high static pressure of 300MPa at 57 ℃ for 120min, taking out, deactivating enzyme at 100 ℃ for 10min, centrifuging at 10000g for 60min, desalting, and drying to obtain the sweet potato peptide.
Example 4 preparation of a Potato active peptide (4)
Cleaning sweet potato, peeling, cutting into blocks, adding 0.45% citric acid aqueous solution (containing Vc concentration of 0.05%) according to a material-liquid ratio of 1:1, pulping, filtering to remove residues, centrifuging to remove starch, ultrafiltering, concentrating, and lyophilizing to obtain sweet potato protein. Mixing sweet potato protein according to the weight ratio of g: 1 mL: 30 in the ratio of the alkaline protease Alcalase and the sweet potato protein are dissolved in Tris-HCl buffer solution with the pH value of 8.3, the sweet potato protein is treated by 200W ultrasonic wave for 5min, then the sweet potato protein is treated by high-pressure homogenization under the pressure of 120MPa for 1min, and the alkaline protease Alcalase and the sweet potato protein are mixed according to the weight ratio of g: 1 mL: 30, packaging, performing enzymolysis at 56 ℃ for 150min under high static pressure of 200MPa, taking out, inactivating enzyme at 90 ℃ for 10min, centrifuging at 10000g for 60min, desalting, and drying to obtain sweet potato peptide.
Example 5 preparation of a Potato active peptide (5)
Cleaning sweet potato, peeling, cutting into blocks, adding 0.3% citric acid aqueous solution (containing Vc concentration of 0.03%) according to the material-liquid ratio of 1:1, pulping, filtering to remove residue, centrifuging to remove starch, ultrafiltering, concentrating, and lyophilizing to obtain sweet potato protein. Mixing sweet potato protein according to the weight ratio of g: 1 mL: 30 in the ratio of the alkaline protease Alcalase and the sweet potato protein are dissolved in Tris-HCl buffer solution with the pH value of 8.3, the sweet potato protein is treated by 200W ultrasonic wave for 5min, then the sweet potato protein is treated by high-pressure homogenization under the pressure of 120MPa for 1min, and the alkaline protease Alcalase and the sweet potato protein are mixed according to the weight ratio of g: 1 mL: 35, packaging, performing enzymolysis at 55 ℃ for 240min under high static pressure of 100MPa, taking out, inactivating enzyme at 90 ℃ for 10min, centrifuging at 9000g for 60min, desalting, and drying to obtain sweet potato peptide.
Example 6 preparation of a Potato active peptide (6)
Cleaning sweet potato, peeling, cutting into blocks, adding 0.25% citric acid aqueous solution (containing Vc concentration of 0.01%) according to the material-liquid ratio of 1:1, pulping, filtering to remove residue, centrifuging to remove starch, ultrafiltering, concentrating, and lyophilizing to obtain sweet potato protein. Mixing sweet potato protein according to the weight ratio of g: 1 mL: 30 in the ratio of the alkaline protease Alcalase and the sweet potato protein are dissolved in Tris-HCl buffer solution with the pH value of 8.3, the sweet potato protein is treated by 200W ultrasonic wave for 5min, then the sweet potato protein is treated by high-pressure homogenization under the pressure of 10MPa for 1min, and the alkaline protease Alcalase and the sweet potato protein are mixed according to the weight ratio of g: 1 mL: 40, packaging, performing enzymolysis at 57 ℃ for 240min under high static pressure of 100MPa, taking out, inactivating enzyme at 90 ℃ for 10min, centrifuging at 8000g for 60min, desalting, and drying to obtain sweet potato peptide.
Comparative example 1
Cleaning sweet potato, peeling, cutting into blocks, adding 0.2% citric acid aqueous solution (containing Vc concentration of 0.1%) according to the material-liquid ratio of 1:1, pulping, filtering to remove residue, centrifuging to remove starch, ultrafiltering, concentrating, and lyophilizing to obtain sweet potato protein. Mixing sweet potato protein according to the weight ratio of g: 1 mL: 30 in Tris-HCl buffer solution with pH value of 8.3, and mixing alkaline protease Alcalase and sweet potato protein according to the ratio of g: 1 mL: 25, packaging, performing enzymolysis at a high static pressure of 300MPa at 57 ℃ for 120min, taking out, deactivating enzyme at 100 ℃ for 10min, centrifuging at 10000g for 60min, desalting, and drying to obtain the sweet potato peptide.
Comparative example 2
Cleaning sweet potato, peeling, cutting into blocks, adding 0.2% citric acid aqueous solution (containing Vc concentration of 0.1%) according to the material-liquid ratio of 1:1, pulping, filtering to remove residue, centrifuging to remove starch, ultrafiltering, concentrating, and lyophilizing to obtain sweet potato protein. Mixing sweet potato protein according to the weight ratio of g: 1 mL: 30 is dissolved in Tris-HCl buffer solution with the pH value of 8.3, sweet potato protein is treated by 200W ultrasonic wave for 5min, and alkaline protease Alcalase and the sweet potato protein are mixed according to the proportion of g: 1 mL: 30, performing enzymolysis at 56 ℃ for 150min, taking out, inactivating enzyme at 90 ℃ for 10min, centrifuging at 10000g for 60min, desalting, and drying to obtain sweet potato peptide.
Comparative example 3
Cleaning sweet potato, peeling, cutting into blocks, adding 0.2% citric acid aqueous solution (containing Vc concentration of 0.1%) according to the material-liquid ratio of 1:1, pulping, filtering to remove residue, centrifuging to remove starch, ultrafiltering, concentrating, and lyophilizing to obtain sweet potato protein. Mixing sweet potato protein according to the weight ratio of g: 1 mL: 30 is dissolved in Tris-HCl buffer solution with pH value of 8.3, sweet potato protein is homogenized for 1min under high pressure of 120MPa, alkaline protease Alcalase and sweet potato protein are mixed according to the proportion of g: 1 mL: 35, carrying out enzymolysis at 55 ℃ for 240min, taking out, inactivating enzyme at 90 ℃ for 10min, centrifuging at 9000g for 60min, desalting, and drying to obtain the sweet potato peptide.
Comparative example 4
Cleaning sweet potato, peeling, cutting into blocks, adding 0.2% citric acid aqueous solution (containing Vc concentration of 0.1%) according to the material-liquid ratio of 1:1, pulping, filtering to remove residue, centrifuging to remove starch, ultrafiltering, concentrating, and lyophilizing to obtain sweet potato protein. Mixing sweet potato protein according to the weight ratio of g: 1 mL: 30 in Tris-HCl buffer solution with pH value of 7.5, and mixing alkaline protease Alcalase and sweet potato protein according to the ratio of g: 1 mL: 25, carrying out enzymolysis at 50 ℃ for 60min, taking out, inactivating enzyme at 100 ℃ for 10min, centrifuging at 10000g for 60min, desalting, and drying to obtain the sweet potato peptide.
Experimental example 1
Degree of hydrolysis, hydroxyl radical scavenging activity, Fe for active peptides in examples and comparative examples2+Chelating power, total antioxidant capacity, amino acid composition and the like:
(1) degree of hydrolysis
The method is carried out by adopting an o-phthalaldehyde method. The degree of hydrolysis is calculated as follows:
h ═ serine NH2- β)/α mmol/g protein
Wherein h corresponds to the number of amino groups that hydrolyze peptide bonds, expressed as millimoles of amino groups of serine. α and β are 1.00 and 0.40, respectively.
Degree of hydrolysis (%) ═ h/htot×100
Wherein h istotThe total number of peptide bonds per protein equivalent. For most protein molecules, htotAbout 8g/kg protein. The results are shown in Table 1.
(2) Hydroxyl radical scavenging Activity
The alpha-deoxyribose oxidation method is adopted. Dissolving active peptide in distilled water to obtain solution with concentration of 1 mg/mL. 0.1mL of 10mM FeSO4·7H2O, 0.9mL of 0.1M phosphate buffer (pH 7.4), 0.5mL of 10mM α -deoxyribose, 0.1mL of 10mM EDTA, and 0.2mL of the sample solution were mixed well in a test tube. 0.2mL of 10mM H was added2O2Then the reaction was started and placed in a 37 ℃ bath for 1 h. After the reaction, 1.0mL of 2.8% TCA (glacial acetic acid) was added to terminate the reaction, 1mL of 1% TBA (50mM NaOH) was added thereto and mixed, followed by development in a boiling water bath for 20min, cooling and measuring the absorbance at 532 nm. OH clearance (%) was calculated as follows:
hydroxyl radical clearance (%) ═ a (a)0－A1)/A0】×100
Wherein: a. the0Absorbance values for the blank control; a. the1The absorbance of the sample after reaction. The results are shown in Table 1.
(3)Fe2+Chelating power
Dissolving active peptide in distilled water to obtain solution with concentration of 1 mg/mL. The reaction mixture included 45. mu.L of 2mM FeCl2450 μ L of sample and 1815 μ L of distilled water. The mixture was shaken vigorously and then left at room temperature for 30 min. After 30min, 90. mu.L of 5mM 4,4' - [3- (2-pyridyl) -1,2, 4-triazine-5, 6-diyl was added]The diphenyl sulfonic acid monosodium salt (ferrozine) is mixed evenly. Determination of Fe at 562nm2+-absorbance of ferrozine complex. Distilled water was used as a blank. Fe2+Chelating capacity (%) was calculated as follows:
Fe2+chelating force (%) ═ a (a)0－A1)/A0】×100
Wherein: a. the0Absorbance values for the blank control; a. the1The absorbance of the sample after reaction. The results are shown in Table 1.
(4) Total antioxidant capacity
The scavenging activity of active peptides on peroxy radicals was determined by the oxygen radical absorbance capacity method (ORAC). All solutions were prepared and diluted with 75mmol/L, pH 7.4 phosphate buffered saline. Adding 20 mu L of a sample to be detected (the concentration is 1mg/mL), 20 mu L of phosphate buffer solution and 20 mu L of 63nmol/L fluorescein sodium solution into a 96 micro-porous plate, preserving the heat at 37 ℃ for 10min, immediately adding 140 mu L of 18.28mmol/L AAPH solution, placing the solution into a multifunctional microplate reader, measuring the fluorescence value under the excitation wavelength of 485nm and the emission wavelength of 535nm, setting the time interval to be 2.0min, measuring the times for 60 times and measuring the temperature at 37 ℃. The fluorescence value of each reaction solution in the absence of AAPH (i.e., the AAPH solution was replaced with an equal amount of phosphate buffer solution) was measured simultaneously using water-soluble vitamin E as a standard, and the oxygen radical absorbance capacity of the sample solution was expressed as μ g water-soluble vitamin E equivalent (TE)/mL sample solution. The results are shown in Table 1.
(5) Analysis of amino acid composition
The amino acid composition of the active peptide is determined by an amino acid automatic analyzer, and specifically comprises the following steps: 75mg of sweet potato peptide was weighed and subjected to enzymatic hydrolysis with 10mL of 6M HCl at 110 ℃ for 24 hours. After hydrolysis, the mixture was poured into a 50mL volumetric flask, and the volume was fixed with ultrapure water, and 1mL of hydrolyzed liquid nitrogen was taken and blown to dryness. Dissolving the dried sample in sodium citrate buffer solution with pH value of 2.2, adjusting the concentration of amino acid to 50-250nmol/mL, and then loading the sample to Hitachi L-8800 amino acid analyzer for amino acid determination. The results are shown in Table 1.
TABLE 1 antioxidant Activity and amino acid composition analysis of active peptides
As can be seen from Table 1, the active peptide of potato species prepared in all the examples and comparative examples has a certain antioxidant activity, the proportion of essential amino acids in the total essential amino acids is more than 40%, and the ratio of essential amino acids to non-essential amino acids is more than 60%, which is obviously higher than the reference mode recommended by FAO/WHO.
Comparison with comparative example 1, the degree of hydrolysis, hydroxyl radical scavenging activity, Fe of the active peptides of examples 1,2 and 32+The chelating force and the total oxidation resistance are obviously improved; examples 4 and 5 degree of hydrolysis, hydroxyl radical scavenging activity, Fe of active peptides2+The chelating force and the total oxidation resistance are obviously higher than those of comparative example 2 and comparative example 3A peptide.
The degree of hydrolysis, hydroxyl radical scavenging activity, Fe of the active peptide of example 6 compared to the active peptide of example 52+Chelating power and total oxidation resistance are slightly low; comparative example 4 hydrolysis degree, hydroxyl radical scavenging Activity, Fe of active peptide2+The chelating power and the total antioxidant capacity are the lowest among all the active peptides mentioned above.
Experimental example 2
The molecular weight distribution of the active peptides in each example and comparative example was analyzed:
a certain amount of the active peptide was dissolved in 50mM phosphate solution (pH7.0) containing 0.5M sodium chloride, filtered through a 0.22 μ M membrane, and subjected to molecular weight distribution measurement by LC-20A HPLC (Shimadzu, Japan) equipped with Superdex peptide 10/300GL column (10X 300 mM). The eluent contained 0.5M sodium chloride in 50mM phosphate solution (pH7.0) at a flow rate of 0.5 mL/min. The absorbance was measured at 215 nm. The molecular weight standard curve was performed using cytochrome C (12384 Da), aprotinin (6512Da), vitamin B12(1855Da) and glycine (75 Da). The results are shown in Table 2.
TABLE 2 molecular weight distribution (%)
As can be seen from table 2, the content of the <3kDa peptide component in the active peptides of examples 1,2 and 3 was significantly increased compared to comparative example 1; the content of the <3kDa peptide component in the active peptides of examples 4 and 5 was significantly higher than the active peptides of comparative examples 2 and 3. The content of the <3kDa peptide component in the active peptide of example 6 was slightly lower compared to the active peptide of example 5; whereas the content of the <3kDa peptide component of the active peptide of comparative example 4 was the lowest among all the active peptides mentioned above.
Although the invention has been described in detail hereinabove with respect to a general description and specific embodiments thereof, it will be apparent to those skilled in the art that modifications or improvements may be made thereto based on the invention. Accordingly, such modifications and improvements are intended to be within the scope of the invention as claimed.
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