Partial Purification of Mussel Adhesive Protein for Mytilus Edulis and Preparation of Mussel Protein Hydrolysates

  • Sun, Nam-Kyu (Department of Food Science and Technology, College of Agriculture, Chungnam National University) ;
  • Song, Kyung-Bin (Department of Food Science and Technology, College of Agriculture, Chungnam National University)
  • Published : 2000.09.01

Abstract

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.