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KMID : 1007520000090060353
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Food Science and Biotechnology
2000 Volume.9 No. 6 p.353 ~ p.357
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Purification and Identification of Angiotensin-1 Converting Enzyme Inhibitory Peptide from Turban Shell (Turbo cornutus)
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Lee, Hyeon Gyu
SHIN, HYUN KYUNG/Kim, Yong Hyun/Yang, Cha Bum/Do, Jeong Ryong
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Abstract
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In order to find the naturally occurring angiotensin-I converting enzyme (ACE) inhibitor, eight types of shellfishes (turban shell, hard shell, corb shell, little neck calm, abalone, oyster, scallop, and ark shell) were studied through the ACE inhibitory assay. Among them, turban shell (turbo cornutus) water extract showed a relatively high inhibitory activity against ACE. ACE inhibitory substance was isolated from turban shell protein, and its structure was identified. The water soluble extract from turban shell protein showed 58.34% ACE inhibitory activity, while those of other organic solvent extracts showed lower ACE inhibitory activities (13.33-25.59%). Turban shell protein hydrolyzate was prepared using Papain 30,000. The lower molecular fraction (less than 10,000 dalton) in the ultrafiltration of turban shell protein hydrolyzate had a higher ACE inhibitory activity. For the isolation of ACE inhibitory peptide, reversed phase column chromatography and gel permeation column chromatography were performed. The highest active fraction of the ACE inhibitory peptide was purified, and its amino acid sequence was identified as Tyr-Val-Glu.
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