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Purification and Characterization of Proteases from Digestive Tract of Grass Shrimp ( Penaeus monodon )
Author(s) -
JIANG SHANNTZONG,
MOODY MICHAEL W.,
CHEN HSINGCHEN
Publication year - 1991
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1991.tb05271.x
Subject(s) - proteases , protease , penaeus monodon , trypsin , hydrolysis , biochemistry , shrimp , casein , enzyme , chymotrypsin , biology , chemistry , fishery
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.