Determination of angiotensin-I converting enzyme inhibitory peptides in chicken leg bone protein hydrolysate with Alcalase.

in Sciences Citation Index(SCI), 科學引文索引資料庫(SCI)
標題Determination of angiotensin-I converting enzyme inhibitory peptides in chicken leg bone protein hydrolysate with Alcalase.
出版類型SCI(Sciences Citation Index)
出版年度2009
AuthorsChih-Ming Chen, 陳志銘, Tien-Chun Wan T. - C. W., Yu-Tse Liu 柳育澤, Fu-Yuan Cheng 鄭富元, Liang-Chuan Lin 林亮全, & Ryoichi Sakata?田亮一
開始頁91
頁數6
出版日期2009 / 2
其他編號0000
中文摘要

This study aims to identify peptides with angiotensin-I converting enzyme (ACE) inhibitory activity in hydrolysate from chicken leg bone protein hydrolyzed with alcalase for 4 h (A4H). The hydrolysate has demonstrated potent in vitro ACE inhibitory activity, and has been shown to attenuate the development of hypertension and cardiovascular hypertrophy in spontaneously hypertensive rats (SHR). A4H is competitive for ACE and was separated using high-performance liquid chromatography (HPLC) with a gel filtration column (Superdex Peptide HR 10/30). The results show that A4H is a mixed non-competitive inhibitor. Eighteen fractions were detected after separation of A4H, and most of them showed ACE inhibitory activity. Five fractions with strong ACE inhibitory activities (above 50%) were labeled from A to E. In addition, there were 10 peptides, consisting of 5–10 amino acid residues that were identified from fraction D that exhibited the strongest ACE inhibitory activity. Three of the identified peptides corresponded to peptides derived from collagen type I and chicken muscular protein. It is revealed that A4H has several peptides that possess ACE inhibitory activities.

期刊名稱Animal Science Journal
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