蛋清源ACE抑制肽结构鉴定及其稳定性  

Characterization and stability of ACE inhibitory peptides derived fromegg white protein

作　　者：刘静波[1] 于志鹏[1] 赵文竹[1] 于一丁[1] 刘博群 林松毅[1] 

机构地区：[1]吉林大学军需科技学院营养与功能食品研究室,长春130062

出　　处：《吉林大学学报（工学版）》2011年第2期579-584,共6页Journal of Jilin University:Engineering and Technology Edition

基　　金：'863'国家高技术研究发展计划项目(2007AA10Z329)

摘　　要：利用碱性蛋白酶酶解蛋清制备活性肽,采用交联葡聚糖凝胶色谱初步纯化具有血管紧张素转化酶抑制活性的组分,高活性组分通过液相色谱-四极杆线性离子阱串联质谱(LC-QTRAP)对纯化组分进行结构鉴定得到19个活性肽。分别对其中3个活性肽DHPFLF、HAEIN和QIGLF进行化学合成及活性测定,其中QIGLF的ACE抑制活性较高,IC50为75.00μM,对胃蛋白酶和胰蛋白酶具有较强的抗酶解能力。Bioactive peptides from egg white were prepared by enzymatic hydrolysis with alkaline proteinase.The fraction with Angiotensin-Converting Enzyme（ACE） inhibition was purified by gel chromatography.Nineteen active peptides were identified by quadruple linearity ion trap tandem mass spectrometry.Three active peptides： DHPFLF,HAEIN and QIGLF were synthesized and the activities were measured.Results show that QIGLF has the highest activity with the IC50 value of 75.00 μM,and was resistant to digestion by protease of the gastrointestinal tract. 更多

关 键 词：食品加工技术 蛋清 血管紧张素转化酶抑制肽 结构鉴定 稳定性 

分 类 号：TS201.2[轻工技术与工程—食品科学]