Journal
APPLIED AND ENVIRONMENTAL MICROBIOLOGY
Volume 75, Issue 17, Pages 5496-5500Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/AEM.01298-09
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Funding
- National High Technology Research and Development Program of China [2006AA10Z402]
- Natural Science Foundation of Jiangsu Province, China [BK2008331]
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A novel esterase gene, pytH, encoding a pyrethroid-hydrolyzing carboxylesterase was cloned from Sphingobium sp. strain JZ-1. The gene contained an open reading frame of 840 bp. Sequence identity searches revealed that the deduced enzyme shared the highest similarity with many alpha/beta-hydrolase fold proteins ( 20 to 24% identities). PytH was expressed in Escherichia coli BL21 and purified using Ni-nitrilotriacetic acid affinity chromatography. It was a monomeric structure with a molecular mass of approximately 31 kDa and a pI of 4.85. PytH was able to transform p-nitrophenyl esters of short-chain fatty acids and a wide range of pyrethroid pesticides, and isomer selectivity was not observed. No cofactors were required for enzyme activity.
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