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食品与发酵工业  2021, Vol. 47 Issue (13): 146-153    DOI: 10.13995/j.cnki.11-1802/ts.026193
  生产与科研应用· 本期目录 | 过刊浏览 | 高级检索 |
蓝圆鲹黄嘌呤氧化酶抑制肽的制备及其活性分析
周雅1,2, 胡晓2*, 李来好2, 杨贤庆2, 陈胜军2, 吴燕燕2, 杨少玲2
1(上海海洋大学 食品学院,上海,201306)
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研究室,广东 广州,510300)
Preparation and characterization of xanthine oxidase inhibitory peptides from round scad (Decapterus maruadsi) muscleZ
HOU Ya1,2, HU Xiao2*, LI Laihao2, YANG Xianqing2, CHEN Shengjun2, WU Yanyan2, YANG Shaoling2
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)
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摘要 以蓝圆鲹为原料,选用胰蛋白酶、木瓜蛋白酶、中性蛋白酶、复合蛋白酶及碱性蛋白酶对其进行水解。以酶解产物黄嘌呤氧化酶(xanthine oxidase,XOD)的抑制活性为指标,通过单因素试验及正交试验确定了最佳的酶解制备条件。结果显示,最佳酶解条件为采用中性蛋白酶,加酶量0.3%(质量分数),料液比1∶2(g∶mL),pH 7.0,酶解温度50 ℃,酶解时间6 h。在此条件下,蓝圆鲹多肽(round scad peptides,RSPs)的XOD抑制活性为64.03%(15 g/L),Fe2+结合活性为61.56%;此法获得的RSPs分子质量92.35%分布在1 000 Da以下;氨基酸分析表明,RSPs中与XOD抑制活性有关的疏水性氨基酸(如Ala、Val、Leu、Ile)以及与金属离子结合活性相关的氨基酸(如Glu、Asp、Arg、His)含量较高;此外,紫外光谱和红外光谱扫描结果表明,RSPs可与Fe2+发生结合反应,其与Fe2+的结合位点可能是酰胺键、氨基的N原子与羧基的O原子。
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周雅
胡晓
李来好
杨贤庆
陈胜军
吴燕燕
杨少玲
关键词:  蓝圆鲹  酶解  制备  黄嘌呤氧化酶抑制肽    
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.
Key words:  round scad (Decapterus maruadsi)    enzymatic hydrolysis    preparation    xanthine oxidase inhibitory peptides
收稿日期:  2020-11-16      修回日期:  2020-12-09           出版日期:  2021-07-15      发布日期:  2021-08-02      期的出版日期:  2021-07-15
基金资助: 财政部和农业农村部:国家现代农业产业技术体系资助项目(CARS-47);中国水产科学研究院基本科研业务费资助项目(2020TD69);广东省基础与应用基础研究基金项目(2019A1515011588);广东省科技创新战略专项资金(纵向协同管理方向)计划项目(2018S0044);广东省重点领域研发计划资助项目(2020B1111030004);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)
作者简介:  硕士研究生(胡晓副研究员为通讯作者,E-mail: hnhuxiao@163.com)
引用本文:    
周雅,胡晓,李来好,等. 蓝圆鲹黄嘌呤氧化酶抑制肽的制备及其活性分析[J]. 食品与发酵工业, 2021, 47(13): 146-153.
HOU Ya,HU Xiao,LI Laihao,et al. Preparation and characterization of xanthine oxidase inhibitory peptides from round scad (Decapterus maruadsi) muscleZ[J]. Food and Fermentation Industries, 2021, 47(13): 146-153.
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