酶解文蛤小分子肽分离纯化及生化特性  

Separation and Purification the Minor Peptides from the Meretrix Linnaeu Protein Hydrolysates and the Investigation of the Biochemical Properties

作　　者：邱春江[1] 姚兴存[1] 赵培培[1] 薛长湖[2] 

机构地区：[1]淮海工学院江苏省海洋生物技术重点建设实验室,江苏连云港222005 [2]中国海洋大学食品科学系,山东青岛266003

出　　处：《食品研究与开发》2010年第5期4-6,共3页Food Research and Development

摘　　要：通过对文蛤胰蛋白酶解物中的小分子肽进行Sephadex G-15凝胶层析,利用Fenton体系测定洗脱液对产生的.OH的清除效果,找出具有活性的抗氧化肽后利用Tricine-SDS-PAGE方法鉴定洗脱液的分离纯度。结果显示：文蛤在酶解温度50℃、pH=8.0~8.5,加酶量为2%,当酶解时间为8 h时所得酶解物对羟自由基清除率不高;仅将酶解时间减半,重复以上操作,所得酶解物对.OH清除率明显提高,达到94.02%,将其经Sephadex G-15凝胶层析后,发现由第3个峰所收集到的洗脱液的清除率最高,电泳结果显示本峰纯度较高。The purpose of this study was to explore the meretrix linnaeu protein hydrolysates with Sephadex G-15,and the scavenging activity（SA）of them on hydroxyl free radical produced by Fenton reaction,find out the antioxidant activity of the peptides.Then investigate the Separation of purity with the Tricine-SDS-PAGE.The result show that the SA of the enzymatic hydrolysates is not very good at time duration 8 h,temperature 50 ℃,pH 8.0-8.5,enzyme content 2 %（w/w）.Then halved the hydrolysis time and made other conditions remain unchanged,its SA is 94.02 %.It shows that the third band has the highest SA and also has the high purity by electrophoresis after the meretrix linnaeu enzymatic hydrolysates with Sephadex G-15.

关 键 词：文蛤 酶解物 活性肽 羟自由基 电泳 

分 类 号：TS254[轻工技术与工程—水产品加工及贮藏工程]