黑豆ACE抑制肽的分离纯化与稳定性研究  

Isolation and stability of black soybean ACE inhibitory peptide

作　　者：杜晓妹 李梅青[1] 周鑫[1] 李芬[1] 

机构地区：[1]安徽农业大学茶与食品科技学院,合肥230036

出　　处：《安徽农业大学学报》2016年第4期516-519,共4页Journal of Anhui Agricultural University

基　　金：合肥农产品加工研究院资助院企合作项目(2012HAPP002)资助

摘　　要：利用大孔吸附树脂DA201-C、超滤和Sephadex G-15凝胶色谱对ACE抑制肽进行分离纯化,并对其稳定性进行研究。结果表明,经过分离纯化后,得到的4个组分均有一定的ACE抑制作用,其中组分ⅢACE抑制率最高为90.78%,其分子量主要集中在145~468 Da;ACE抑制肽具有较好的p H（2~10）、金属离子（Ca2＋、K＋和Mg2＋）和温度（〈40℃）稳定性,但发现其抗消化稳定性不强,属于底物型ACE抑制肽。该结果可为进一步研究和开发黑豆的ACE抑制肽提供参考。ACE inhibitory peptide in black soybean was isolated and purified using DA201-C resin, ultrafiltration and Sephadex G-15 gel filtration chromatography. Its stability was further studied. Four fractions with ACE inhibitory activity were separated and purified in which fraction III had the highest activity that was 90.78%. The molecular weight of the peptide was 145-468 Da. ACE inhibitory peptide was stable in the high pH, metal ion and thermo （〈40℃） condition, while it was of substrate type with weak stability against gastrointestinal proteases. The results would provide a reference for further studying and developing black soybean ACE inhibitory peptide.

关 键 词：ACE抑制肽 分离纯化 稳定性 

分 类 号：TS201.21[轻工技术与工程—食品科学]