A Novel Thermostable Esterase from the Thermoacidophilic Archaeon Sulfolobus Tokodaii Strain 7

Overview

Journal FEMS Microbiol Lett

Publisher Oxford University Press

Specialty Microbiology

Date 2004 Jun 24

PMID 15212797

Citations 15

Authors

Yoichi Suzuki

Kenji Miyamoto

Hiromichi Ohta

Affiliations

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Abstract

We have characterized an esterase expressed from the putative esterase gene (ST0071) selected from the total genome analysis from the thermoacidophilic archaeon Sulfolobus tokodaii strain 7. The ORF was cloned and expressed as a fusion protein in Escherichia coli. The protein was purified with heat treatment, affinity column chromatography, and size exclusion filtration. The optimum activity for ester cleavage against p-nitrophenyl esters was observed at around 70 degrees C and pH 7.5-8.0. The enzyme exhibited high thermostability and also showed activity in a mixture of a buffer and water-miscible organic solvents, such as acetonitrile and dimethyl sulfoxide. From the kinetic analysis, p-nitrophenyl butyrate was found to be a better substrate than caproate and caprylate.

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