This study was supported by American Institute in Taiwan (AIT) and Council of Agriculture of R.O.C under Grant No. FG-Ta-120 (TW-AES-27).
Purification and Characterization of Proteases from Digestive Tract of Grass Shrimp (Penaeus monodon)
Version of Record online: 25 AUG 2006
Journal of Food Science
Volume 56, Issue 2, pages 322–326, March 1991
How to Cite
JIANG, S.-T., MOODY, M. W. and CHEN, H.-C. (1991), Purification and Characterization of Proteases from Digestive Tract of Grass Shrimp (Penaeus monodon). Journal of Food Science, 56: 322–326. doi: 10.1111/j.1365-2621.1991.tb05271.x
- Issue online: 25 AUG 2006
- Version of Record online: 25 AUG 2006
- Ms received 10/20/89/ revised 7/25/90; accepted 9/10/90.
Proteases in grass shrimp (Penaeus monodon) digestive tract were extracted. Four fractions, A, B, C and D, demonstrated caseinolytic activity and were purified to electrophoretic homogeneity. A, C and D were trypsin-like, while B was a chymotrypsin-like protease. Optimal temperature for proteases A, B and C were 65°C, and that for D was 55°C for hydrolysis of casein. Optimal pH of proteases A and C was 8.0, and that of D was 7.0 for hydrolysis of p-toluenesulfonyl-L-arginine methyl ester. Optimal pH of protease B for hydrolysis of N-benzoyl-L-tyrosine ethyl ester was 8.0. Inactivation of 50 % enzyme activity in 5 min occurred at 67°C for protease B and 50°C for proteases A, C and D.