本文已被：浏览 5263次 下载 3555次
投稿时间：2016-08-03
投稿时间：2016-08-03
中文摘要: 采用 Protamex蛋白酶水解鱼胶原蛋白源制备血管紧张素转化酶（ACE）抑制肽，并采用 pH-stat 法测定水解 度，对影响水解效果的 pH 值、温度、底物浓度和加酶量 4 个因素进行考察，并进行三元二次通用旋转设计进行优化，对 活性肽的 ACE 抑制活性和结构进行分析。结果表明在底物浓度 11.8 %，pH 8.7，加酶量 5.4 %和酶解温度 53.6 ℃条件下， 酶解 1 h 所得的鱼皮胶原蛋白水解度为 16.6 %，经高效液相测定鱼皮 ACE 抑制活性为 45 %，经圆二色谱分析鱼胶原蛋 白 ACE 抑制肽主要以无规卷曲形式存在。
Abstract:Fish-derived collagen was hydrolyzed by protamex protease and measured by the degree of hydrol－ ysis. The hydrolysis model of peptides from fish-derived collagen was established through quadratic general ro－ tation design followed single factor experiment， subsequently ACE inhibitory activity and secondary structure of fish collagen-derived peptides was measured. The results showed that the equation for the optimal regression e－ quation had a maximal value according to regression coefficient test， regression equation， and the lack of fit test. The optimal details of enzymatic hydrolysis was followed： substrate concentration 11.8 %， enzymatic hy－ drolysis pH value 8.7， the amount of enzyme 5.4 % and hydrolysis temperature 53.6 ℃， and hydrolysis degree of fish-derived collagen was 16.6 % in one hour. In vitro ACE inhibitory activity of bioactive peptides from fish-derived collagen was performed by high performance liquid chromatography， and the value of activity a－ gainst ACE was 45 %. In addition， secondary structure of fish collagen-derived ACE inhibitory peptide was random coil.
keywords: fish-derived collagen angiotensin converting enzyme（ACE） bioactive peptide secondary structure
文章编号：201707013 中图分类号：10.3969/j.issn.1005-6521.2017.07.013 文献标志码：A
基金项目:国家科技支撑课题（2012BAD00B03）；辽宁省科学事业公益研究基金项目（2016004004）；渤海大学博士启动项目（0515bs079）；辽宁 省科技攻关项目（2015103020）
| 作者 | 单位 |
| 于志鹏1，张霜1，赵文竹1，*，张倩1，沈俊彤1，王瑜1，霍倩倩1，励建荣1，*，刘静波 | 1. 渤海大学 食品科学与工程学院，生鲜农产品贮藏加工及安全控制技术国家地方联合工程研究中心，辽宁 锦州 121013；2. 吉林大学 营养与功能食品研究室，吉林 长春 130062 |
引用文本：
津ICP备20000603号-1