Abstract
Alkaline proteases from the viscera of the striped seabream (Lithognathus mormyrus) were extracted and characterized. Interestingly, the crude enzyme was active over a wide range of pH from 6.0 to 11.0, with an optimum pH at the range of 8.0-10.0. In addition, the crude protease was stable over a broad pH range (5.0-12.0). The optimum temperature for enzyme activity was 50 °C. The crude alkaline proteases showed stability towards various surfactants and bleach agents and compatibility with some commercial detergents. It was stable towards several organic solvents and retained more than 50% of its original activity after 30 days of incubation at 30 °C in the presence of 25% (v/v) dimethyl sulfoxide, N,N-dimethylformamide, diethyl ether, and hexane. The crude enzyme extract was also tested for shrimp waste deproteinization in the preparation of chitin. The protein removal with a ratio enzyme/substrate of 10 was about 79%.
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