基于模拟酶切的酪蛋白定向酶解探究  

Study on directed enzymatic preparation from casein based on simulated peptide-cut

作　　者：彭莉娟[1] 王伟[2] 张赛赛[1] 赵春江[1] 冯凤琴[1] 

机构地区：[1]浙江大学生工食品学院,浙江杭州310058 [2]浙江省农业科学院,浙江杭州310021

出　　处：《食品工业科技》2012年第3期214-216,321,共4页Science and Technology of Food Industry

基　　金：浙江省重大科技项目(2006C12096);863项目(2008AA10Z313)

摘　　要：用模拟酶切软件peptidecutter提供的39种蛋白酶,对已知序列的酪蛋白进行模拟酶切,以生成的寡肽数量为指标建立酶解肽库,选择适用酶并进行真实条件下的酶解验证,获得最适用酶;以血管紧张素转化酶(ACE)抑制肽的抑制率和酪蛋白磷酸肽(CPP)的氮磷摩尔比来评价ACE抑制肽的活性及CPP的纯度,超滤分离酶解液获得高纯度的ACE抑制肽和CPP。结果表明:胰蛋白酶为最适用酶,超滤后ACE抑制肽的抑制活性及CPP的纯度显著升高(p<0.01),获得了高活性的ACE抑制肽和高纯度的CPP。Caseins with known sequences were simulated peptide-cut into small peptides by 39 kinds of proteases using the software of peptidecutter,and the suitable effective proteases were chosen in terms of the amount of oligo-peptides and enzymatic peptide library was established.The most effective protease was determined in the confirmatory experiment.Angiotensin Ⅰ-converting enzyme inhibitory peptides（ACEIPs） and CPPs were obtained after ultra-filtration,and the inhibitory activity of ACEIP and the N/P ratio of CPP were used to assess the activity of ACEIP and the purity of CPP.The results implied that：the trypsin was chosen as the most suitable protease.Compared with the mixture before ultra-filtration,the activity of ACEIP and the purity of CPP were extremely significant improved（p〈0.01）.In this way,higher activity of ACEIPs and higher purity of CPPs were obtained.

关 键 词：酪蛋白 模拟酶解 血管紧张素转化酶(ACE)抑制肽 酪蛋白磷酸肽(CPP) 

分 类 号：TS201.21[轻工技术与工程—食品科学]