食品与发酵工业 >

2021 , Vol. 47 >Issue 23: 185 - 192

DOI: https://doi.org/10.13995/j.cnki.11-1802/ts.027276

生产与科研应用

卵形鲳鲹黄嘌呤氧化酶抑制肽的制备及其工艺优化

  • 侯梦凡 ,
  • 胡晓 ,
  • 杨贤庆 ,
  • 陈胜军 ,
  • 吴燕燕 ,
  • 许加超
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  • 1(中国海洋大学 食品科学与工程学院,山东 青岛,266003)
    2(中国水产科学研究院 南海水产研究所,农业农村部水产品加工重点实验室,广东 广州,510300)
硕士研究生(杨贤庆研究员和许加超教授为共同通讯作者,E-mail:yxqgd@163.com;xujia@ouc.cn)

收稿日期: 2021-03-15

  修回日期: 2021-04-10

  网络出版日期: 2021-12-31

基金资助

现代农业产业技术体系建设专项(CARS-47);茂名市引进创新创业团队项目(200201095834980);广东省基础与应用基础研究基金项目(2019A1515011588);广东省重点领域研发计划项目(2020B020226005,2020B1111030004);中国水产科学研究院基本科研业务费资助项目(2020TD69);中国水产科学研究院南海水产研究所中央级公益性科研院所基本科研业务费专项(2021SD06);山东省重大科技创新工程项目(2019JZZY020613);青岛市科技惠民专项(20-3-4-31-nsh)

收起

Preparation and process optimization of xanthine oxidase inhibitory peptides from Trachinotus ovatus

  • HOU Mengfan ,
  • HU Xiao ,
  • YANG Xianqing ,
  • CHEN Shengjun ,
  • WU Yanyan ,
  • XU Jiachao
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  • 1(College of Food Science and Engineering,Ocean University of China,Qingdao 266003,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: 2021-03-15

  Revised date: 2021-04-10

  Online published: 2021-12-31

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摘要

以卵形鲳鲹为原料,采用不同蛋白酶对其进行水解以制备黄嘌呤氧化酶(xanthine oxidase,XOD)抑制肽。以水解度和XOD抑制活性为评价指标,在单因素试验的基础上结合响应面法优化了酶解法制备XOD抑制肽的工艺,并对酶解产物的分子质量分布和氨基酸组成进行了分析。结果表明中性蛋白酶为最适用酶,确立的最佳酶解工艺条件为:料液比1∶3(g∶mL),酶解温度54 ℃,pH 7.0,酶解3.85 h,加酶量0.19%。在此条件下测得水解度和XOD抑制活性值分别为11.82%和52.41%,与预测值基本一致。该法制备所得的XOD抑制活性肽主要以分子质量<3 000 Da的组分为主,占比为93.92%,其疏水氨基酸占比高达36.95%,亮氨酸、丙氨酸、缬氨酸和异亮氨酸含量较高。该研究可为卵形鲳鲹的精深加工和高值化利用提供指导。

关键词： 卵形鲳鲹; 黄嘌呤氧化酶抑制肽; 多肽; 酶解工艺; 肽分子质量; 氨基酸分析

本文引用格式

侯梦凡 , 胡晓 , 杨贤庆 , 陈胜军 , 吴燕燕 , 许加超 . 卵形鲳鲹黄嘌呤氧化酶抑制肽的制备及其工艺优化[J]. 食品与发酵工业, 2021 , 47(23) : 185 -192 . DOI: 10.13995/j.cnki.11-1802/ts.027276

Abstract

In this study, Trachinotus ovatus muscle was hydrolyzed with different proteases to obtain xanthine oxidase (XOD) inhibitory peptides. The degree of hydrolysis and the XOD inhibition activity were used as evaluation index, and the optimum hydrolysis conditions were obtained by single factor analysis and response surface methodology. Then, the molecular weight distribution and amino acids composition of the hydrolysates were investigated. The results showed that neutral protease was the optimal enzyme, and the optimum hydrolysis conditions were as follows: the solid-liquid ratio of 1∶3 (g∶mL), the hydrolysis temperature of 54 ℃ and pH 7.0 for 5 h, with the enzyme dosage of 0.19%. Under these conditions, the hydrolysis degree and XOD inhibitory activity were 11.82% and 52.41% respectively, which was consistent with the predicted values. The molecular weight of the peptides obtained by this method was mainly less than 3 000 Da (account for 93.92%). Its hydrophobic amino acid content was as high as 36.95%, and rich in Leu, Ala, Val and Ile. The results provide reference for the intensive processing and high-value utilization of T.ovatus.

Key words： Trachinotus ovatus; xanthine oxidase inhibitory peptides; polypeptide; enzymatic hydrolysis process; molecular weight of peptide; amino acid analysis

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