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KMID : 1160620000050030148
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Preventive Nutrition and Food Science
2000 Volume.5 No. 3 p.148 ~ p.152
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Partial Purification of Mussel Adhesive Protein for Mytilus Edulis and Preparation of Mussel Protein Hydrolysates
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Sun Nam-Kyu
Song Kyung-Bin
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Abstract
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Mussel adhesive protein (MAP) was extracted from Korean Mytilus edulis and then partially purified using Sephacryl S-300 gel permeation chromatography and reversed-phase high performance liquid chromatography. As an indicator of adhesiveness, is 3,4-dihydroxyphenylalanine (DOPA) content was determined. Its DOPA/protein ratio of 0.19 was higher than those of other reports, indicating a good adhesive. The partially purified MAP was confirmed by acid-urea polyacrylamide gel electrophoresis using cetylpiridinium bromide as a cationic detergent. Sea mussel hydrolysates were prepared using three commercial proteases to provide value-added functional materials and their angiotensin converting enzyme (ACE) inhibitory activities were determined. Among hydrolysates of sea mussel, Protamex was the best and further purification would improved ACE inhibitory activity.
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KEYWORD
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mussel adhesive protein, Mytilus edulis, protein hydrolysates, ACE inhibitor
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