Preparation and characterization of xanthine oxidase inhibitory peptides from round scad (Decapterus maruadsi) muscleZ

  • HOU Ya ,
  • HU Xiao ,
  • LI Laihao ,
  • YANG Xianqing ,
  • CHEN Shengjun ,
  • WU Yanyan ,
  • YANG Shaoling
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  • 1(College of Food Science and Technology,Shanghai Ocean University,Shanghai 201306,China)
    2(Key Laboratory of Aquatic Product Processing,Ministry of Agriculture and Rural Affairs,South China Sea Fisheries Research Institute,Chinese Academy of Fishery Science,Guangzhou 510300,China)

Received date: 2020-11-16

  Revised date: 2020-12-09

  Online published: 2021-08-02

Abstract

Round scad (Decapterus maruadsi) muscle was hydrolyzed with five different proteases (trypsin, papain, neutrase, protomax and alcalase). The optimum conditions of enzymatic hydrolysis were obtained by single factor analysis and orthogonal test by the index of xanthine oxidase (XOD) inhibition activity. The optimum conditions of enzymatic hydrolysis were as follows: neutrase of 0.3% (mass fraction), the solid-liquid ratio of 1∶2 (g∶mL), pH 7.0, 50 ℃, and 6 h. Under the optimal conditions, the XOD inhibition activity of round scad peptides (RSPs) was 64.03% (15 g/L) and the Fe2+ chelating activity was 61.56%. The molecular weight of RSPs was 92.35% distributed below 1 000 Da. The analysis of amino acids showed that the content of hydrophobic amino acids related to XOD inhibition activity (such as Ala, Val, Leu, Ile) and metal ion binding activity (such as Glu, Asp, Arg, His) accounted for more. In addition, ultraviolet spectrum and Fourier transform infrared spectroscopy demonstrated that RSPs could bound with Fe2+, and the possible binding sites were located at amide bonds, nitrogen atom of the amino group or oxygen atom of the carboxyl group.

Cite this article

HOU Ya , HU Xiao , LI Laihao , YANG Xianqing , CHEN Shengjun , WU Yanyan , YANG Shaoling . Preparation and characterization of xanthine oxidase inhibitory peptides from round scad (Decapterus maruadsi) muscleZ[J]. Food and Fermentation Industries, 2021 , 47(13) : 146 -153 . DOI: 10.13995/j.cnki.11-1802/ts.026193

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