Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 49, Issue 6, Pages 3004-3009Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jf001135r
Keywords
angiotensin I converting enzyme inhibitory peptide; fermented soybean paste; preparative HPLC; hypertension; spontaneously hypertensive rats
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It has been reported that soybean peptide fractions isolated from Korean fermented soybean paste exert angiotensin I converting enzyme (ACE) inhibitory activity in vitro. In this study, further purification and identification of the most active fraction inhibiting ACE activity were performed, and its antihypertensive activity in vivo was confirmed. Subsequently, a novel ACE inhibitory peptide was isolated by preparative HPLC. The amino acid sequence of the isolated peptide was identified as His-His-Leu (HHL) by Edman degradation. The IC50 value of the HHL for ACE activity was 2.2 mug/mL in vitro. Moreover, the synthetic tripeptide HHL (spHHL) resulted in a significant decrease of ACE activity in the aorta and led to lowered systolic blood pressure (SBP) in spontaneously hypertensive (SH) rats compared to control. Triple injections of spHHL, 5 mg/kg of body weight/ injection resulted in a significant decrease of SEP by 61 mmHg (p < 0.01) after the third injection. These results demonstrated that the ACE inhibitory peptide HHL derived from Korean fermented soybean paste exerted antihypertensive activity in vivo.
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