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Purification and identification of an ACE inhibitory peptide from the peptic hydrolysate of Acetes chinensis and its antihypertensive effects in spontaneously hypertensive rats  ( SCI-EXPANDED收录)   被引量:34

文献类型:期刊文献

英文题名:Purification and identification of an ACE inhibitory peptide from the peptic hydrolysate of Acetes chinensis and its antihypertensive effects in spontaneously hypertensive rats

作者:Cao, Wenhong[1];Zhang, Chaohua[1];Hong, Pengzhi[1];Ji, Hongwu[1];Hao, Jiming[1]

机构:[1]Guangdong Ocean Univ, Coll Food Sci & Technol, Zhanjiang 524025, Guangdong, Peoples R China

年份:2010

卷号:45

期号:5

起止页码:959

外文期刊名:INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY

收录:SCI-EXPANDED(收录号:WOS:000276606900014)、、WOS

基金:This work was supported by funds from the Science &Technology Exploration Plan Research Funding of Guangdong Ocean University (No. 0912047).

语种:英文

外文关键词:Acetes chinensis; angiotensin I-converting enzyme inhibitory peptide; antihypertensive effect; enzymatic hydrolysis

外文摘要:P>Acetes chinensis is a marine shrimp found in the coastal waters of China. The shrimp was hydrolysed by pepsin to prepare hydrolysates with angiotensin I-converting enzyme (ACE) inhibitory activity. The hydrolysate with the highest ACE inhibitory activity resulted from a 3-5 h incubation at 45 degrees C and pH 2.5 with pepsin. Gel filtration and RP-HPLC were used to separate ACE inhibitory peptides from the hydrolysate. The gel filtration fraction of the hydrolysate with a molecular weight range from 1320 Da to 311 Da exerted the highest ACE inhibition activity. This fraction was separated by RP-HPLC into fifteen fractions, of which fraction F9 showed 92.7% of the ACE inhibition activity. Its peptide sequence was determined to be Leu-His-Pro. It showed a potent antihypertensive activity in spontaneously hypertensive rats. The results suggested that this peptide may be a potent ACE inhibitor which might be developed into a healthy food to lower blood pressure.

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