A novel thermostable esterase from the thermoacidophilic archaeon Sulfolobus tokodaii strain 7 | Zendy

Yuka Suzuki | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

A novel thermostable esterase from the thermoacidophilic archaeon Sulfolobus tokodaii strain 7

Author(s) -

Yuka Suzuki

Publication year - 2004

Publication title -

fems microbiology letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.899

H-Index - 151

eISSN - 1574-6968

pISSN - 0378-1097

DOI - 10.1016/j.femsle.2004.05.026

Subject(s) - thermostability , esterase , sulfolobus , dimethyl sulfoxide , escherichia coli , size exclusion chromatography , biochemistry , enzyme , biology , chromatography , chemistry , gene , organic chemistry , archaea

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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research