詹炜君,金星鹏,陈俪锟,陈 丽.马鲛鱼黄嘌呤氧化酶抑制肽的制备工艺优化及抗氧化活性研究[J].食品安全质量检测学报,2023,14(22):278-287
马鲛鱼黄嘌呤氧化酶抑制肽的制备工艺优化及抗氧化活性研究
Preparation process optimization and antioxidant activity of xanthine oxidase inhibitory peptide from Scomberomorus niphonius
投稿时间:2023-08-24  修订日期:2023-11-24
DOI:
中文关键词:  马鲛鱼  酶解  超声  黄嘌呤氧化酶
英文关键词:Scomberomorus niphonius  enzymatic hydrolysis  ultrasound  xanthine oxidase
基金项目:江苏省海洋科技创新专项项目(HY2018-10)、江苏省“333工程”高层次人才培养资金资助项目(BRA2014111)、连云港市“521高层次人才培养工程”资助项目(LYG52105-2018028)、江苏省海洋生物产业技术协同创新中心专项资金资助项目
作者单位
詹炜君 江苏海洋大学药学院 
金星鹏 江苏海洋大学药学院 
陈俪锟 江苏海洋大学药学院 
陈 丽 江苏海洋大学江苏省海洋资源开发研究院 
AuthorInstitution
ZHAN Wei-Jun College of Pharmacy, Jiangsu Ocean University 
JIN Xing-Peng College of Pharmacy, Jiangsu Ocean University 
CHEN Li-Kun College of Pharmacy, Jiangsu Ocean University 
CHEN Li Jiangsu Ocean University Jiangsu Marine Resources Development and Research Institute 
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中文摘要:
      目的 探究马鲛鱼黄嘌呤氧化酶抑制肽制备的最佳条件及其抗氧化活性。方法 以马鲛鱼为原料, 黄嘌呤氧化酶抑制肽采用超声辅助酶法制备, 并筛选最佳反应用酶; 以单因素实验为基础, 通过Box-Behnken响应面分析法, 以黄嘌呤氧化酶抑制活性为响应值, 优化得到酶解最优条件。通过1,1-二苯基-2-三硝基苯肼(1,1-diphenyl-2-picrylhydrazyl, DPPH)自由基清除等方法测定膜分离物的抗氧化活性。结果 最佳反应用酶为复配的中性蛋白酶与复合蛋白酶(1:1, m:m)。优化所得的最佳酶解条件为: 酶解温度50℃, 加酶量为0.2%, pH为7.0。在此条件下黄嘌呤氧化酶抑制率37.49%, 与回归理论模型基本符合。3个组分的膜分离物中, 相对分子量小于1 kDa的酶解产物的抗氧化性能力最强。结论 本研究制备的黄嘌呤氧化酶抑制肽对黄嘌呤氧化酶有较好的抑制作用, 且抗氧化性良好, 为工业化制备马鲛鱼黄嘌呤氧化酶抑制肽提供了数据基础和理论依据。
英文摘要:
      Objective To investigate the optimal preparation conditions and antioxidant activity of xanthine oxidase inhibitory peptides from Scomberomorus niphonius. Methods The xanthine oxidase inhibitory peptides were prepared by ultrasound-assisted enzymatic method with Scomberomorus niphonius as raw material, and the best enzymes were screened by Box-Behnken response surface analysis based on single-factor experiments, the xanthine oxidase inhibitory activity was used as the response value to optimize the enzymatic hydrolysis conditions. The antioxidant activity of membrane isolates was determined by 1,1-diphenyl-2-picrylhydrazyl free radical scavenging methods. Results The best reaction enzyme was the compound neutral protease and compound protease (1:1, m:m). The optimum conditions were as follows: Temperature 50℃, enzyme dosage 0.2%, pH 7.0. Under these conditions, the xanthine oxidase inhibition rate was 37.49%, which was consistent with the regression model. Among the 3 components, the enzymatic hydrolysates with relative molecular weight less than 1 kDa had the strongest antioxidant activity. Conclusion The xanthine oxidase inhibitory peptide prepared in this study has a good inhibitory effect on xanthine oxidase and good antioxidant activity, which provides the data basis and theoretical basis for the industrial preparation of xanthine oxidase inhibitory peptide of mackerel.
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