Journal
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
Volume 97, Issue -, Pages 225-232Publisher
ELSEVIER
DOI: 10.1016/j.molcatb.2013.07.022
Keywords
Carboxylesterase; Thermophilic; Sulfolobus tokodaii; Bacterial lipase and esterase; Pyrethroid
Funding
- National Natural Science Foundation of China [1176229]
- Key Science and Technology Project of Henan Province [132102110197]
- Research Foundation of Zhengzhou University of Light Industry [000544]
- Zhengzhou Key Laboratory of Industrial Biotechnology
- State Key Laboratory of Microbial Technology at Shandong University
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A novel gene ST2026 encoding a putative carboxylesterase from the thermophilic crenarchaeota Sulfolobus tokodaii (named EstSt7) was cloned and functionally overexpressed in Escherichia coli. The recombinant enzyme was purified to homogeneity after heat treatment, Ni-NTA affinity and Superdex-200 gel filtration chromatography. EstSt7 showed maximum activity at 80 degrees C over 30 min and had a half-life of 180 min at 90 degrees C. Its enzymatic activity was stable in the pH range of 8.0-10.0 with an optimum at 9.0. The enzyme exhibited significant esterase activity toward various p-nitrophenyl esters and the most preferable substrate was p-nitrophenyl butyrate (k(cat)/K-m of 246.3 s(-1) mM(-1)). In addition, EstSt7 showed high activity and stability against organic solvents (20% and 50% v/v) and detergents (1% and 5% v/v). Furthermore, EstSt7 could efficiently hydrolyze a wide range of synthetic pyrethroids including fenpropathrin, permethrin, cypermethrin, cyhalothrin, deltamethrin and bifenthrin, which makes it a potential candidate for the detoxification of pyrethroids for the purpose of biodegradation. Sequence alignment, phylogenetic analysis and comparison of the conserved motif reveal that this novel carboxylesterase EstSt7 should be grouped into a new bacterial lipase and esterase family. (C) 2013 Elsevier B.V. All rights reserved.
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