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KMID : 1160620000050020075
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Preventive Nutrition and Food Science
2000 Volume.5 No. 2 p.75 ~ p.80
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Purification and Characterization of Angiotensin I-Converting Enzyme Inhibitors from Sinapis alba L.
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Yuk Jin-Su
Lim Young-Hee
Cho Hong-Yon
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Abstract
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To separate ACE inhibitors from edible plants, spices, and herbs, 285 extracts of 95 sources were screened for ACE inhibitory activity. The extract of Sinapis alba L. had the most potent ACE inhibitory activity. Mustard seeds were crushed homogeneously and extracted with hexane and water successively. Lyophilized water extract was fractionated with H₂O: butanol (1:1). The ACE inhibitor was purified from butanol fraction by methanol precipitation, gel filtration, HPLC, and FPLC with Superdex peptide HQ 10/30 column. The active fraction has been purified to homogeneity, which was proven by gel filtration using FPLC system. The yield was 0.02%. The compound has a molecular weight of about 640. The compound competitively inhibited ACE activity and the IC_(50) value was 79 ㎍/ml. The purified compound showed uterus contraction activity in isolated rat uterus.
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KEYWORD
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angiotensin converting enzyme, inhibitor, Sinapis alba, uterus contraction activity
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