Abstract
Trypsin was purified from the pyloric ceca of spotted mackerel (Scomber australasicus) by gel filtration on Sephacryl S-200 and Sephadex G-50. The purification and yield were 20-fold and 81%, respectively, as compared to those in the starting crude extract. Final enzyme preparation was nearly homogeneous in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and the molecular weight of the enzyme was estimated to be 24,000 Da by SDS-PAGE. The trypsin was stable at pH 5-11 for 30 min at 30C, and its maximal activity against N a -p-tosyl-L-arginine methyl ester was pH 8.0. Trypsin was heat-stable up to about 50C for 15 min at pH 8.0. Optimum temperature of the trypsin enzyme was 60C. The enzyme was stabilized by calcium ion. The purified trypsin was strongly inhibited by serine protease inhibitors such as N-p-tosyl-L-lysine chloromethyl ketone and soybean trypsin inhibitor, suggesting that it is a trypsin-like serine protease. N-Terminal amino acid sequence of spotted mackerel trypsin was IVGGYECTAHSQPHQVSLNS.
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