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.
出处
《安徽农业大学学报》
CAS
CSCD
北大核心
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
关键词
ACE抑制肽
分离纯化
稳定性
ACE Inhibitory Peptides
Purification
Stability
