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CN-122012658-A - Method for improving stabilizing activity and antioxidant activity of chicken peptide ADH and polypeptide and application thereof

CN122012658ACN 122012658 ACN122012658 ACN 122012658ACN-122012658-A

Abstract

The invention discloses a method for improving chicken peptide ADH stabilizing activity and antioxidant activity, and polypeptide and application thereof. According to the invention, the ADH stabilizing activity and the antioxidant activity of the chicken peptide can be improved by performing a plastein reaction on the chicken peptide, and the addition of exogenous amino acid in the plastein reaction can be proved for the first time to further and obviously improve the ADH stabilizing activity and the antioxidant activity of the chicken peptide, and compared with the unreacted chicken peptide and the chicken peptide subjected to the plastein reaction, the ADH stabilizing activity and the antioxidant activity of the prepared product are obviously improved by at least 105%, wherein under the action of alkaline protease and the plastein reaction of cysteine, leucine, tryptophan and lysine, the ADH stabilizing activity and the antioxidant activity of the chicken peptide are obviously improved. The method provided by the invention is simple, convenient and quick, the prepared polypeptide product has obvious effect, and more product raw material sources with better effects are provided.

Inventors

  • Xiao Chuqiao
  • XIAO JIE
  • Zeng Hujiaan
  • Lang Jizhou
  • LI XIANGGUANG

Assignees

  • 广东工业大学

Dates

Publication Date
20260512
Application Date
20251226

Claims (10)

  1. 1. A method for improving the stabilizing activity and the antioxidant activity of chicken peptide ADH, which is characterized by comprising the following steps: S1, preparing chicken peptide, namely cutting chicken breast, adding distilled water with the volume of 0.8-10 times of that of the chicken breast, mixing, adjusting the pH value, adding 0.01-10% alkaline protease, hydrolyzing for 0.5-72 hours, centrifuging after enzyme deactivation, collecting supernatant, and freeze-drying to obtain the chicken peptide; S2, adding 0.01-10% protease into chicken peptide with the concentration of 15-50%, adjusting the pH value to 6-11, and carrying out shake hydrolysis for 0.5-72 h at 15-70 ℃; Or S2, adding 0.01-10% protease into chicken peptide with the concentration of 15-50%, simultaneously adding 1-10% amino acid, adjusting the pH value to 6-11, and carrying out shake hydrolysis for 0.5-72 h at 15-70 ℃; S3, inactivating enzyme after Plastein reaction is completed, centrifuging, taking supernatant, and freeze-drying or spray-drying the polypeptide powder.
  2. 2. The method of claim 1, wherein the protease in S2 is selected from alkaline protease, papain or neutral protease.
  3. 3. The method of claim 1, wherein the amino acid in S2 is selected from the group consisting of cysteine, leucine, tryptophan, lysine, proline, and alanine.
  4. 4. The method of claim 1, wherein the concentration of the chicken peptide in S2 is 25-35%.
  5. 5. The method of claim 1, wherein the concentration of the amino acid in S2 is 3-8%.
  6. 6. Use of the method according to any one of claims 1-5 for the preparation of a polypeptide product having high ADH stabilizing and antioxidant activity.
  7. 7. A chicken peptide prepared by the method of any one of claims 1-6.
  8. 8. Use of the chicken peptide of claim 7 for the preparation of an ADH-activated product and/or an antioxidant product.
  9. 9. Use of the chicken peptide of claim 7 in the preparation of a product for alleviating alcoholic liver injury.
  10. 10. An ADH-activated product and/or an antioxidant product comprising the chicken peptide of claim 7.

Description

Method for improving stabilizing activity and antioxidant activity of chicken peptide ADH and polypeptide and application thereof Technical Field The invention relates to the technical field of polypeptide preparation and biological medicine, in particular to a method for improving chicken peptide ADH stabilizing activity and antioxidant activity, and a polypeptide and application thereof. Background The transproteinic reaction (plastein reaction), also known as a proteinoid reaction, is a proteolytic and resynthetic reaction catalyzed by proteases. Essentially, an enzyme is a reverse-directed hydrolysis that catalyzes the religation of fragments following cleavage of a peptide chain by a proteolytic enzyme at a specific high concentration (typically > 20%) of the substrate to form a new, larger or structurally altered polypeptide product, thereby altering the structure and function of the polypeptide. The plastin reaction is mainly used for (1) enhancing/endowing biological activity by recombining or introducing specific groups, enhancing activities of polypeptide such as oxidation resistance, ACE inhibition, antibiosis, mineral combination and the like, (2) improving nutrition and physical properties such as eliminating bad flavor and bitter taste, improving solubility, emulsifying property and foam stability, improving safety of sensitized proteins, (3) upgrading and utilizing protein resources, namely converting low-value proteins (such as fish processing offcut and oil meal) into high-value, digestible and good-flavor functional protein ingredients, (4) synthesizing customized structural peptide which is used as a biocatalysis tool to synthesize peptide segments with specific sequences or structures under mild conditions for scientific research or medical precursors, and (5) being used for a drug delivery system, wrapping hydrophobic active substances (such as vitamins, polyphenols and drugs) by utilizing the characteristic that the peptide segments can form hydrophobic aggregates, and improving stability and bioavailability. Because of the high randomness, weak targeting and unpredictable limitation of the conventional Plastein reaction, the prior researches generally adopt a chemical modification method (such as PEGylation) and utilize chemical reaction to connect modification groups so as to improve the stability and half-life, but the reaction conditions are severe, the activity can be damaged, and the toxic risk of the reagent can also exist. Prior studies have altered polypeptide structure and enhanced activity by introducing amino acids. As disclosed in the prior art, the addition of cysteine in Plastein reaction can raise DPPH free radical clearance rate of chicken lung peptide by 51.85%, OH clearance rate by 31.30%, and heat stability of chicken lung peptide, and heat denaturation temperature of chicken lung peptide from 122.06 ℃ to 136.15 ℃. However, there are few Plastein reaction methods and reports for increasing ADH (alcohol dehydrogenase) activity. The present application was made in order to further enhance the ADH stabilizing activity and oxidation resistance of chicken-derived polypeptides. Disclosure of Invention The invention aims to solve the technical problem of improving the ADH stabilizing activity and oxidation resistance of the existing chicken source polypeptide, and provides a method for improving the chicken peptide ADH stabilizing activity and oxidation resistance, and a polypeptide and application thereof. It is a first object of the present invention to provide a method for increasing the stabilizing and antioxidant activity of the chicken peptide ADH. A second object of the present invention is to provide the use of the above method. A third object of the present invention is to provide a chicken peptide. A fourth object of the present invention is to provide a chicken peptide application as described above. It is a fifth object of the present invention to provide a product. The above object of the present invention is achieved by the following technical scheme: the invention provides a method for improving the stabilizing activity and the antioxidant activity of chicken peptide ADH, which comprises the following steps: S1, preparing chicken peptide, namely cutting chicken breast, adding distilled water with the volume of 0.8-10 times of that of the chicken breast, mixing, adjusting the pH value, adding 0.01-10% alkaline protease, hydrolyzing for 0.5-72 hours, centrifuging after enzyme deactivation, collecting supernatant, and freeze-drying to obtain the chicken peptide; S2, adding 0.01-10% protease into chicken peptide with the concentration of 15-50%, adjusting the pH value to 6-11, and carrying out shake hydrolysis for 0.5-72 h at 15-70 ℃; Or S2, adding 0.01-10% protease into chicken peptide with the concentration of 15-50%, simultaneously adding 1-10% amino acid, adjusting the pH value to 6-11, and carrying out shake hydrolysis for 0.5-72 h at 15-70 ℃; S3, inactivat