Food Science and Technology Research
Online ISSN : 1881-3984
Print ISSN : 1344-6606
ISSN-L : 1344-6606
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Galloylated Catechins as Potent Inhibitors of Angiotensin Converting Enzyme
Zhe LiuToshiyuki NakamuraShintaro MunemasaYoshiyuki MurataYoshimasa Nakamura
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2016 Volume 22 Issue 6 Pages 847-851


In the present study, we investigated the inhibitory effects of four tea catechins, including (−)-epicatechin (EC), (−)-epigallocatechin (EGC), (−)-epicatechin gallate (ECg) and (−)-epigallocatechin gallate (EGCg), on angiotensin converting enzyme (ACE) activity in vitro. Each catechin treatment significantly reduced the ACE activity with the order of potency being EGCg > ECg > EGC = EC. The addition of 1 mM borate significantly recovered the reduced ACE activities by tea catechins, suggesting that hydroxyl groups at the B-ring or at a galloyl moiety play an important role in the ACE-inhibitory mechanism. The covalent modification of ACE by tea catechins was also observed by a redox-cycling staining experiment. A Lineweaver-Burk plot indicated that EGC and ECg were non-competitive inhibitors. The galloylated catechins might more potently inhibit ACE activity in an allosteric manner through the interaction of the galloyl moiety with the non-catalytic site of ACE.

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© 2016 by Japanese Society for Food Science and Technology
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