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Purification and identification of novel xanthine oxidase inhibitory peptides derived from round scad (Decapterus maruadsi) protein hydrolysates

Purification and identification of novel xanthine oxidase inhibitory peptides derived from round scad (Decapterus maruadsi) protein hydrolysates

Hu, Xiao, Zhou, Ya, Zhou, Shaobo ORCID logoORCID: https://orcid.org/0000-0001-5214-2973, Chen, Shengjun, Wu, Yanyan, Li, Laihao and Yang, Xianqing (2021) Purification and identification of novel xanthine oxidase inhibitory peptides derived from round scad (Decapterus maruadsi) protein hydrolysates. Marine Drugs, 19 (10):538. pp. 1-14. ISSN 1660-3397 (doi:10.3390/md19100538)

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Abstract

The objective of the present study was to investigate the xanthine oxidase (XO) inhibitory effects of peptides purified and identified from round scad (Decapterus maruadsi) hydrolysates (RSHs). In this study, RSHs were obtained by using three proteases (neutrase, protamex and alcalase). Among them, the RSHs of 6-h hydrolysis by neutrase displayed the strongest XO inhibitory activity and had an abundance of small peptides (<500 Da). Four novel peptides were purified by immobilized metal affinity chromatography and identified by nano-high-performance liquid chromatography mass/mass spectrometry. Their amino acid sequences were KGFP (447.53 Da), FPSV (448.51 Da), FPFP (506.59 Da) and WPDGR (629.66 Da), respectively. Then the peptides were synthesized to evaluate their XO inhibitory activity. The results indicated that the peptides of both FPSV (5 mM) and FPFP (5 mM) exhibited higher XO inhibitory activity (22.61 ± 1.81% and 20.09 ± 2.41% respectively). Fluorescence spectra assay demonstrated that the fluorescence quenching mechanism of XO by these inhibitors (FPSV and FPFP) was a static quenching procedure. The study of inhibition kinetics suggested that the inhibition of both FPSV and FPFP was reversible, and the type of their inhibition was a mixed one. Molecular docking revealed the importance of π-π stacking between Phe residue (contained in peptides) and Phe914 (contained in the XO) in the XO inhibitory activity of the peptides.

Item Type: Article
Additional Information: This article belongs to the Special Issue Bioactive Peptides from Marine By-Products and Underused Marine Organisms.
Uncontrolled Keywords: round scad (Decapterus maruadsi); hydrolysis; peptides; xanthine oxidase inhibitory; purification; identification
Subjects: Q Science > Q Science (General)
R Medicine > RA Public aspects of medicine > RA0421 Public health. Hygiene. Preventive Medicine
R Medicine > RM Therapeutics. Pharmacology
Faculty / School / Research Centre / Research Group: Faculty of Engineering & Science
Faculty of Engineering & Science > School of Engineering (ENG)
Last Modified: 24 Mar 2023 10:03
URI: http://gala.gre.ac.uk/id/eprint/39036

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