Open AccessA novel thermostable esterase from the thermoacidophilic archaeon Sulfolobus tokodaii strain 7
Author(s) -
Suzuki Yoichi,
Miyamoto Kenji,
Ohta Hiromichi
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 - 10.1111/j.1574-6968.2004.tb09633.x
Subject(s) - sulfolobus , strain (injury) , psychrophile , esterase , biology , archaea , enzyme , genetics , bacteria , biochemistry , anatomy
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 °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.