Journal
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
Volume 83, Issue 5, Pages 882-891Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1080/09168451.2019.1574555
Keywords
Bacillus thermocloaceae; carboxylesterase; thermostability
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Funding
- GIST research institute (GRI) in 2018
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A novel thermostable carboxylesterase (Est5250) of thermoalkaliphilic bacterium Bacillus thermocloaceae was heterologously expressed in Escherichia coli and its biochemical properties were investigated. Est5250 showed optimum esterase activity at 60 degrees C and pH 8.0. The enzyme was highly thermostable at 60 degrees C, interestingly, the thermostability was enhanced in the presence of Ca2+, retaining more than 60% of its original activity after 12 h of pre-incubation. Est5250 was active in the presence of 1% (v/v) of organic solvents and 0.1% (v/v) of non-ionic detergents. The enzyme activity was significantly enhanced up to 167% and 159% in the presence of 2-mercaptoethanol and dithiothreitol, respectively. Est5250 showed high substrate specificity for short-chain p-nitrophenyl-esters. Kinetic constants, K-m and k(cat), for p-nitrophenyl-acetate were 185.8 mu M and 186.6 s(-1), respectively. Est5250 showed outstanding thermostability and tolerance to various organic solvents under thermoalkaliphilic conditions, suggesting that it would be a highly suitable biocatalyst for various biotechnological applications.
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