Galloylated catechins as potent inhibitors of angiotensin converting enzyme

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7 Citations (Scopus)


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 noncompetitive 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.

Original languageEnglish
Pages (from-to)847-851
Number of pages5
JournalFood Science and Technology Research
Issue number6
Publication statusPublished - 2016


  • Angiotensin converting enzyme
  • Covalent modification
  • Non-competitive inhibition
  • Tea catechins

ASJC Scopus subject areas

  • Biotechnology
  • Food Science
  • Chemical Engineering(all)
  • Industrial and Manufacturing Engineering
  • Marketing


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