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KMID : 1007520000090050292
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Food Science and Biotechnology
2000 Volume.9 No. 5 p.292 ~ p.296
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Purification and Identification of Angiotensin-1 Converting Enzyme Inhibitory Peptide from Small Red Bean Protein Hydrolyzate
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Lee, Hyeon Gyu
Yang, Cha Bum/Kwon, Young Sook/Shin, Hyung Kyung
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Abstract
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Angiotensin-I converting enzyme (ACE) inhibitor was isolated from small red bean protein, and its structure was identified. The water-soluble extract from small red bean flour showed 61.96% ACE inhibitory activity, while that of other organic solvent extracts showed lower ACE inhibitory activities (4.80-14.78%). Small red bean protein hydrolyzate was prepared by hydrolyzing the small red bean protein isolate using seven different proteases. Pepsin was the best enzyme for preparing a protein hydrolyzate with high ACE inhibitory activity. The lower molecular weight fraction (less than 10,000 dalton) in the ultrafiltration of small red bean protein hydrolyzate showed a higher ACE inhibitory activity. For isolation of the ACE inhibitory peptide, column chromatographies such as SP Sephadex C-25, ODS-AQ 120-S50, Sephadex LH-20 and high performance liquid chromatography were performed. The highest active fraction of the ACE inhibitory peptide was purified, and its amino acid sequence was identified as Val-Gly-Leu-Pro-Ile-Phe.
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