期刊
CURRENT PHARMACEUTICAL BIOTECHNOLOGY
卷 9, 期 4, 页码 307-314出版社
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/138920108785161578
关键词
angiotensin converting enzyme; silkworm pupae protein; Bombyx mori; hypertension; hydrolyze
资金
- Program 111 of Ministry of Education of P. R. China
- Program Nation Science and Technology Support Plan of Eleventh Five Year Programming of P. R. China [2006BAD05A01-]
Silkworm pupae protein is a good source of high quality protein. The hydrolyzates of silkworm pupae protein catalyzed by neutrase, pepsin, acidic protease (Asperqiius usamii NO. 537), flavourzyme, alcalase, and trypsin with inhibitory activity on angiotensin I-converting enzyme (ACE) were identified by HPLC. The hydrolyzates catalyzed by acidic protease exerted the highest inhibitory activity on ACE. The hydrolyzing conditions were optimized by one-factor, factional factorial (FFD), and center composite (CCD) design methods, and response surface methodology (RSM). Statistical analyses showed that regression of the second-order model equation is suitable to describe ACE inhibitory bioactivity. The predicted inhibitory activity of hydrolyzates on ACE was 73.5 % at a concentration of 2.0 mg/ml. Optimized RSM technique decreased IC50 of hydrolyzates inhibiting ACE to 1.4 mg/mL from 2.5mg/ml. The molecular weight of the components of the hydrolyzates with inhibitory activity on ACE varied from less than 500 to about 1000 Da by ultra-filter analysis. These studies suggest that hydrolyzates of silkworm protein contain ACE inhibitory activity that could form a potential source of ACE inhibitor drugs.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据