文献类型：期刊文献

英文题名：Angiotensin i converting enzyme inhibitory activity and antihypertensive effect in spontaneously hypertensive rats of cobia (Rachycentron canadum) head papain hydrolysate

作者：Yang, Ping[1]; Jiang, Yuchuan[1]; Hong, Pengzhi[1]; Cao, Wenhong[1]

机构：[1] College of Food Science and Technology, Guangdong Ocean University, Zhanjiang, Guangdong Province, China

年份：2013

卷号：19

期号：3

起止页码：209

外文期刊名：Food Science and Technology International

收录：EI(收录号：20132216373632)

语种：英文

外文关键词：Hydrolysis - Rats - Blood pressure - Enzyme activity

外文摘要：Cobia head protein hydrolysate (CHPH) with angiotensin I converting enzyme (ACE) inhibitory activity was prepared with papain. The 3 kDa ultrafiltration filtrate CHPH-IV of the hydrolysate exerted a potent ACE inhibitory activity with IC50 being 0.24 mg/mL. The fractions with molecular weight located between 1749 Da and 173 Da represented up 66.96% of CHPH-IV, and those between 494 Da and 173 Da represented up 31.37% of CHPH-IV. It was found that the ACE inhibitory activity of CHPH-IV was intensified from IC50 0.24 mg/mL to 0.17 mg/mL after incubation with gastrointestinal proteases. The CHPH-IV significantly decreased the systolic blood pressure in a dose-dependent manner after oral administration to spontaneously hypertensive rats (SHR) at dose of 150 mg/kg, 600 mg/kg and 1200 mg/kg body weight. These results suggested that CHPH-IV from cobia head protein hydrolysate by papain could serve as a source of peptides with antihypertensive activity in functional food industry. ? The Author(s) 2012 Reprints and permissions: sagepub.co.uk/journalsPermissions.nav.