Purification and Identification of Novel Xanthine Oxidase Inhibitory Peptides Derived from Round Scad ( Decapterus maruadsi ) Protein Hydrolysates

The objective of the present study was to investigate the xanthine oxidase (XO) inhibitory effects of peptides purified and identified from round scad ( ) hydrolysates (RSHs). In this study, RSHs were obtained by using three proteases (neutrase, protamex and alcalase). Among them, the RSHs of 6-h hy...

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Published in:Marine drugs 2021-09, Vol.19 (10), p.538
Main Authors: Hu, Xiao, Zhou, Ya, Zhou, Shaobo, Chen, Shengjun, Wu, Yanyan, Li, Laihao, Yang, Xianqing
Format: Article
Language:English
Subjects:
Affinity chromatography
Amino acid sequences
Amino acids
Animals
Aquatic Organisms
Chromatography
Chromatography, High Pressure Liquid
Decapterus maruadsi
Disease
DNA
Enzyme Inhibitors - chemistry
Enzymes
Fish Proteins - chemistry
Fishes
Fluorescence
High performance liquid chromatography
HPLC
Hydrolysates
hydrolysis
Hypertension
Identification
Kinetics
Liquid chromatography
Marine fishes
Mass spectrometry
Mass spectroscopy
Metals
Molecular docking
Molecular Docking Simulation
Peptides
Protein Hydrolysates - chemistry
Protein purification
Proteins
purification
Quenching
Rheumatism
round scad (Decapterus maruadsi)
Subtilisin
Uric acid
Water purification
Xanthine oxidase
Xanthine Oxidase - antagonists & inhibitors
xanthine oxidase inhibitory
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Yang, Xianqing
description The objective of the present study was to investigate the xanthine oxidase (XO) inhibitory effects of peptides purified and identified from round scad ( ) 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 (
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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 (&lt;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 Phe (contained in the XO) in the XO inhibitory activity of the peptides.</description><identifier>ISSN: 1660-3397</identifier><identifier>EISSN: 1660-3397</identifier><identifier>DOI: 10.3390/md19100538</identifier><identifier>PMID: 34677437</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Affinity chromatography ; Amino acid sequences ; Amino acids ; Animals ; Aquatic Organisms ; Chromatography ; Chromatography, High Pressure Liquid ; Decapterus maruadsi ; Disease ; DNA ; Enzyme Inhibitors - chemistry ; Enzymes ; Fish Proteins - chemistry ; Fishes ; Fluorescence ; High performance liquid chromatography ; HPLC ; Hydrolysates ; hydrolysis ; Hypertension ; Identification ; Kinetics ; Liquid chromatography ; Marine fishes ; Mass spectrometry ; Mass spectroscopy ; Metals ; Molecular docking ; Molecular Docking Simulation ; Peptides ; Protein Hydrolysates - chemistry ; Protein purification ; Proteins ; purification ; Quenching ; Rheumatism ; round scad (Decapterus maruadsi) ; Subtilisin ; Uric acid ; Water purification ; Xanthine oxidase ; Xanthine Oxidase - antagonists &amp; inhibitors ; xanthine oxidase inhibitory</subject><ispartof>Marine drugs, 2021-09, Vol.19 (10), p.538</ispartof><rights>2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). 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source Open Access: PubMed Central; Publicly Available Content Database
subjects Affinity chromatography
Amino acid sequences
Amino acids
Animals
Aquatic Organisms
Chromatography
Chromatography, High Pressure Liquid
Decapterus maruadsi
Disease
DNA
Enzyme Inhibitors - chemistry
Enzymes
Fish Proteins - chemistry
Fishes
Fluorescence
High performance liquid chromatography
HPLC
Hydrolysates
hydrolysis
Hypertension
Identification
Kinetics
Liquid chromatography
Marine fishes
Mass spectrometry
Mass spectroscopy
Metals
Molecular docking
Molecular Docking Simulation
Peptides
Protein Hydrolysates - chemistry
Protein purification
Proteins
purification
Quenching
Rheumatism
round scad (Decapterus maruadsi)
Subtilisin
Uric acid
Water purification
Xanthine oxidase
Xanthine Oxidase - antagonists & inhibitors
xanthine oxidase inhibitory
title Purification and Identification of Novel Xanthine Oxidase Inhibitory Peptides Derived from Round Scad ( Decapterus maruadsi ) Protein Hydrolysates
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