摘要
研究酶解米糠蛋白中具有ACE抑制活性短肽组分及其序列,本实验采用等电点沉淀法提取米糠蛋白,经胃蛋白酶、胰蛋白酶、木瓜蛋白酶等单独或联合水解米糠蛋白,并采用Sephadex G-15凝胶层析和SP-Sephadex C-25离子交换层析分离各酶解组分。ACE抑制活性检测结果显示:酶解组分中含有较高抑制活性成分,其相对分子量在500单位以内。各组中活性最高的组分进行HPLC-MS分析,其中活性最高的胃蛋白酶联合胰蛋白酶酶解活性组分主要为Arg-Tyr、Met-Trp、Gly-Val-Tyr或Gly-Asp-Phe,其共同特征是C端具有苯环样结构,提示:这种环结构可能是ACE抑制剂的重要结构特征。
To get the structure and function information about ACEI（angiotensin coverting enzyme） inhibitors derived from food protein. The present study prepared ACEI inhibitors from rice bran. The method of isoelectric point （PI） precipitation was adopted to obtain rice bran protein, which was hydrolyzed by pepsin, trypsin, and papain individually or jointly. The hydrolyzed products were separated according to the differences of molecular weights by Sephadex G-15 gel chromatogram. The components with the highest ACE inhibitor activity measured by FAPGG methods, were separated further by SP-Sephadex C-25. HPLC-MS analysis showed that the highest inhibiting activity comes from pepsin-trypsin digested components, which containing short peptides such as Arg-Tyr, Met-Trp, Gly-Val-Tyr or Gly-Asp-Phe with the common characteristics of phenyl ring-like structure which maybe the important structural charecteristics.
出处
《食品科学》
EI
CAS
CSCD
北大核心
2007年第3期223-227,共5页
Food Science
作者简介
刘志国（1963-），男，教授，博士，研究方向为蛋白质结构与功能以及天然产物研究。
