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KMID : 1007519990080030172
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Food Science and Biotechnology
1999 Volume.8 No. 3 p.172 ~ p.178
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Purification and Identification of Angiotensin - I Converting Enzyme Inhibitory Peptide from Kidndy Bean Protein Hydrolyzate
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SHIN, HYUN KYUNG
KWON, DAE YOUNG/Yang, Cha Bum/Lee, Jung Ran
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Abstract
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Angiotensin-I converting enzyme (ACE) inhibitor was isolated from kidney bean (Phaseolus vulgaris L.) protein and its structure was identified. The water soluble extract from kidney bean flour showed 51.0% ACE inhibitory activity, while other organic solvent extracts showed lower ACE inhibitory activities (12.9∼44.1 %). Kidney bean protein hydrolyzate was prepared by hydrolyzing the kidney bean protein isolate using 7 different proteases. Pepsin was the best enzyme for preparing protein hydrolyzate with the high ACE inhibitory compound. The lower molecular fraction (less than 10,000 dalton) in the ultrafiltration of kidney bean protein hydrolyzate had the higher ACE inhibitory activity. For isolation of ACE inhibitory peptide, column chromatography such as ion-exchange (SP Sephadex C-25), gel filtration (Sephadex LH-20), and reverse-phase high performance liquid chromatography were performed. The molecular mass of the ACE inhibitory peptide peak identified by electrospray-mass spectrometry was 633.09 and its amino acid sequence was Val-Ile-Pro-Ala-Ala-Tyr (calculated molecular weight, 632.80 dalton), which was revealed as a novel sequence for the ACE inhibitory peptide.
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