Purification and Identification of Novel Xanthine Oxidase Inhibitory Peptides Derived from Round Scad (Decapterus maruadsi) Protein Hydrolysates
文献类型： 外文期刊
作者： Hu, Xiao 1 ; Zhou, Ya 1 ; Zhou, Shaobo 4 ; Chen, Shengjun 1 ; Wu, Yanyan 1 ; Li, Laihao 1 ; Yang, Xianqing 1 ;
作者机构： 1.Chinese Acad Fishery Sci, South China Sea Fisheries Res Inst, Key Lab Aquat Prod Proc, Minist Agr & Rural, Guangzhou 510300, Peoples R China
2.Jiangsu Ocean Univ, Coinnovat Ctr Jiangsu Marine Bioind Technol, Lianyungang 222005, Peoples R China
3.Shanghai Ocean Univ, Coll Food Sci & Technol, Shanghai 201306, Peoples R China
4.Univ Bedfordshire, Inst Biomed & Environm Sci & Technol, Sch Life Sci, Luton LU1 3JU, Beds, England
5.Collaborat Innovat Ctr Prov & Minist Coconstruct, Dalian 116034, Peoples R China
关键词： round scad (Decapterus maruadsi); hydrolysis; peptides; xanthine oxidase inhibitory; purification; identification
期刊名称：MARINE DRUGS （ 影响因子：5.118； 五年影响因子：5.951 ）
ISSN：
年卷期： 2021 年 19 卷 10 期
页码：
收录情况： SCI
摘要： 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 & PLUSMN; 1.81% and 20.09 & PLUSMN; 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 pi-pi stacking between Phe residue (contained in peptides) and Phe(914) (contained in the XO) in the XO inhibitory activity of the peptides.
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