Abstract
This study reports biochemical features of a novel esterase of Bacillus sp. HP 96 isolated from Bazangan Lake in Iran. The optimum pH and temperature for 53.4 kDa-purified esterase were 8 and 40 °C, respectively. The HPLC technique was used to examine the main compound produced by the enzyme on nitrophenyl derivatives. Vmax and Km of esterase towards 4-nitrophenyl butyrate (p-NPB) were 75.12 µmol.min−1 mg−1 and 4.66 mM, respectively. Organic solvents (15, 30% v/v) did not have a significant effect on the stability of the purified enzyme. The Bacillus sp. HP 96 esterase showed a high compatibility towards various ionic liquids and detergents. In conclusion, the characterized esterase has potential to be used in detergent formularizations and biotechnological processes under harsh conditions.
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