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Accessible Unlicensed Requires Authentication Published by De Gruyter February 10, 2015

Assessment and Separation of Angiotensin I-Converting Enzyme Inhibitory Peptides in Chinese Soypaste

Fengjuan Li, Kohji Yamaki, Yongqiang Cheng and Yuanyuan Fang

Abstract

A Chinese soypaste-derived fraction with potent angiotensin I-converting enzyme (ACE) inhibitory activity (IC50 = 25.9 μg/mL) was obtained by treating soypaste extract with 80% ethanol. The result of gradient reversed-phase high-performance liquid chromatography (RP-HPLC) suggested that bioactive peptides bearing some polarity groups made a substantial contribution to the ACE inhibitory activity. By mass spectrometric analysis, a component was separated as Glu-Ser-Gly-Asp which was then found to act in a dose-dependent manner against ACE activity as a non-competitive inhibitor, with an IC50 value of 2.297 mM.

Funding statement: Funding: This work was supported by Kirin Holdings Co., Ltd. (former Kirin Brewery Co., Ltd.), Tokyo, during UNU-Kirin Fellowship Programme at National Food Research Institute (NFRI), Tsukuba, Japan, in 2012–13, and its Follow-Up Project in 2013–15. This work was also within the framework of the fund project (Grant No. 31101329) entitled “Generation mechanism of angiotensin-converting enzyme inhibitors in traditional soypaste” from National Natural Science Foundation of China (NSFC).

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Published Online: 2015-2-10
Published in Print: 2015-4-1

©2015 by De Gruyter