Purification and characterization of a novel angiotensin I-converting enzyme inhibitory peptide derived from abalone (Haliotis discus hannai Ino) gonads

Published: 27 August 2014

Author: Qiang Wu, Qiu-Feng Cai, Zhi-Peng Tao, Le-Chang Sun, Jian-Dong Shen, Ling-Jing Zhang, Guang-Ming Liu & Min-Jie Cao

Journal: European Food Research and Technology

Abstract

Abalone gonads were hydrolyzed using alcalase followed by papain to produce angiotensin I-converting enzyme (ACE) inhibitory peptides. Gel filtration column chromatography analysis showed that the molecular weight of the fraction with high ACE inhibitory activity was below 1 kDa, which occupied 93.1 % of total hydrolysate. The ACE inhibitory peptide was purified by a series of column chromatographies, and the sequence of purified peptide was further identified as Ala–Met–Asn (AMN) by automated Edman degradation method. The triple peptide was then synthesized and had an ACE inhibitory activity with IC50 value of 106.24 μg/mL. After gastrointestinal digestion, the peptide still remained bioactivity. Lineweaver–Burk plots indicated that AMN acts as a non-competitive inhibitor against ACE. Our present study suggested that AMN derived from abalone gonad by-products may be used as an ideal nutrient for development of functional foods.  Go to Article Link