Abstract
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.
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