CN-121991169-A - Phycobiliprotein source xanthine oxidase inhibitory peptide and preparation method and application thereof

Abstract

The application relates to phycobiliprotein source xanthine oxidase inhibitory peptide, a preparation method and application thereof, belonging to the technical field of bioactive peptides and functional foods. The phycobiliprotein source xanthine oxidase inhibitory peptide has an amino acid sequence of Ile-Gly-Tyr-Tyr-Leu-Arg or Leu-Asp-Tyr-Tyr-Leu-Arg, and the amino acid sequence is shown as SEQ ID NO.1 or SEQ ID NO. 2. The phycobiliprotein xanthine oxidase inhibitory peptide provided by the application is an important protein resource and a high-quality source of bioactive peptide in spirulina, has wider application, has lower molecular weight, is safer and more efficient, has no toxic or side effect and is easy to digest and absorb compared with a chemically synthesized preparation, and the phycobiliprotein xanthine oxidase inhibitory peptide and xanthine oxidase have high binding affinity, can form a very stable ligand receptor complex and has excellent inhibitory performance on xanthine oxidase.

Inventors

• FU PENGCHENG
• ZHU ZHIMIN

Assignees

• 海南大学

Dates

Publication Date

20260508

Application Date

20260228

Claims (8)

1. 1. The phycobiliprotein source xanthine oxidase inhibitory peptide is characterized in that the amino acid sequence is Ile-Gly-Tyr-Tyr-Leu-Arg or Leu-Asp-Tyr-Tyr-Leu-Arg, and the amino acid sequence table is shown as SEQ ID NO.1 or SEQ ID NO. 2.
2. 2. The phycobiliprotein source xanthine oxidase inhibitory peptide of claim 1, having an amino acid sequence lie-Gly-Tyr-Leu-Arg, abbreviated IGYYLR, molecular formula C 38 H 57 N 9 O 9 , molecular weight 783.91 Da.
3. 3. The phycobiliprotein-derived xanthine oxidase inhibitory peptide of claim 2, wherein the phycobiliprotein-derived xanthine oxidase inhibitory peptide has inhibitory activity on xanthine oxidase and has an IC50 value of 5.062 mM; the phycobiliprotein source xanthine oxidase inhibitory peptide has a concentration of 1-10 mM, and the inhibition rate of xanthine oxidase is 22.009-96.205%.
4. 4. The phycobiliprotein-derived xanthine oxidase inhibitor peptide according to claim 1, characterized in that the amino acid sequence of the phycobiliprotein-derived xanthine oxidase inhibitor peptide is Leu-Asp-Tyr-Leu-Arg, abbreviated as LDYYLR, with molecular formula C 40 H 59 N 9 O 11 and molecular weight 841.95 Da.
5. 5. The phycobiliprotein-derived xanthine oxidase inhibitory peptide of claim 4, wherein the phycobiliprotein-derived xanthine oxidase inhibitory peptide has inhibitory activity on xanthine oxidase and has an IC50 value of 3.824 mM; the phycobiliprotein source xanthine oxidase inhibitory peptide has a concentration of 1-10 mM, and the inhibition rate of xanthine oxidase is 13.313-95.452%.
6. 6. A method for producing the phycobiliprotein-derived xanthine oxidase inhibitory peptide according to any one of claims 1-5, comprising the steps of: Extracting phycobiliprotein source xanthine oxidase inhibitory peptide from phycobiliprotein of spirulina by solid phase synthesis or directional biological enzymolysis and purification.
7. 7. The use of the phycobiliprotein-derived xanthine oxidase inhibitory peptide according to any one of claims 1-5 for preparing a medicament or food for preventing or improving hyperuricemia.
8. 8. The use according to claim 7, wherein the prevention or improvement of hyperuricemia is a xanthine oxidase inhibitory effect.

Description

Phycobiliprotein source xanthine oxidase inhibitory peptide and preparation method and application thereof Technical Field The application relates to the technical field of bioactive peptides and functional foods, in particular to phycobiliprotein source xanthine oxidase inhibitory peptide, and a preparation method and application thereof. Background Xanthine oxidase (xanthine oxidase, XO) is a key enzyme in the purine metabolic pathway and is capable of catalyzing the conversion of xanthine to uric acid. When XO activity is abnormally increased, uric acid production in the body is increased, so that diseases such as hyperuricemia, gout and the like are caused. The traditional XO inhibitor commonly used in clinic mainly comprises allopurinol, febuxostat and other small molecular compounds, but the XO inhibitor is easy to generate problems of hepatotoxicity, skin adverse reaction or drug interaction and the like in the long-term use process, so that the development of safer XO inhibitors with natural sources becomes a research hotspot. In recent years, the proteolytic peptide is widely used for developing functional products such as antioxidation, blood pressure reduction, immunoregulation and the like due to the characteristics of high safety, abundant structural diversity, easier absorption in organisms and the like. Various natural protein sources have been shown to contain short peptides that inhibit XO activity, but their research has focused mainly on common sources of whey protein, fish collagen, soy protein, and the like. Algae proteins, particularly phycobiliprotein (phycobiliprotein), are considered as a potential source of novel bioactive peptides as water-soluble pigment proteins in microalgae, are rich in excellent amino acid composition, and have good safety in the food industry. Phycobiliprotein hydrolysate has a certain research foundation in aspects of antioxidation, anti-inflammation, metabolic regulation and the like, but related reports on xanthine oxidase inhibitory peptides of phycobiliprotein sources are limited at present, and particularly, the application exploration aiming at specific site peptide sequences, accurate preparation methods and application exploration in uric acid reducing directions is lacking. Therefore, the development of the functional peptide which is derived from phycobiliprotein, has a definite amino acid sequence and obvious XO inhibitory activity has important significance for enriching the source of natural uric acid-reducing active substances, expanding the high-value utilization of algae resources and developing novel functional foods or health-care products. Disclosure of Invention In view of the above, the present application provides a phycobiliprotein source xanthine oxidase inhibitory peptide, a preparation method and an application thereof, wherein the phycobiliprotein source xanthine oxidase inhibitory peptide can significantly inhibit XO activity, can be used for regulating purine metabolism and reducing uric acid production, and can effectively overcome the defects of the prior art. The first aspect of the application provides a phycobiliprotein xanthine oxidase inhibitory peptide, the amino acid sequence of which is Ile-Gly-Tyr-Tyr-Leu-Arg or Leu-Asp-Tyr-Tyr-Leu-Arg, and the amino acid sequence is shown as SEQ ID NO.1 or SEQ ID NO. 2. Specifically, SEQ ID NO.1 is Ile-Gly-Tyr-Tyr-Leu-Arg, and SEQ ID NO.2 is Leu-Asp-Tyr-Tyr-Leu-Arg. Ile represents english name Isoleucine, chinese name isoleucine; gly represents that the English name is Glycine and the Chinese name is Glycine; tyr is named as Tyrosine, and Chinese is named as Tyrosine; leu represents English name Leucine and Chinese name leucine; Arg is named as Arginine, and Chinese is named as Arginine; Asp is given by English name ASPARTATE and Chinese name aspartic acid. Preferably, the phycobiliprotein source xanthine oxidase inhibitory peptide has an amino acid sequence of Ile-Gly-Tyr-Tyr-Leu-Arg, abbreviated as IGYYLR, and a molecular formula of C 38H57N9O9 and a molecular weight of 783.91 Da. Preferably, the phycobiliprotein source xanthine oxidase inhibitory peptide has inhibitory activity on xanthine oxidase and has an IC50 value of 5.062 mM; the phycobiliprotein source xanthine oxidase inhibitory peptide has a concentration of 1-10 mM, and the inhibition rate of xanthine oxidase is 22.009-96.205%. Preferably, the phycobiliprotein source xanthine oxidase inhibitory peptide has an amino acid sequence of Leu-Asp-Tyr-Tyr-Leu-Arg, abbreviated as LDYYLR, and a molecular formula of C 40H59N9O11 and a molecular weight of 841.95 Da. Preferably, the phycobiliprotein source xanthine oxidase inhibitory peptide has inhibitory activity on xanthine oxidase and has an IC50 value of 3.824 mM; the phycobiliprotein source xanthine oxidase inhibitory peptide has a concentration of 1-10 mM, and the inhibition rate of xanthine oxidase is 13.313-95.452%. The second aspect of the present application also provides