TY - JOUR
T1 - A novel thermostable esterase from the thermoacidophilic archaeon Sulfolobus tokodaii strain 7
AU - Suzuki, Yoichi
AU - Miyamoto, Kenji
AU - Ohta, Hiromichi
N1 - Funding Information:
This study was supported by Special Coordination Funds for Promoting Science and Technology from Ministry of Education, Culture, Sports, Science and Technology, the Japanese Government.
PY - 2004/7/1
Y1 - 2004/7/1
N2 - 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.
AB - 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.
KW - Archaeon
KW - Recombinant fusion protein
KW - Sulfolobus tokodaii
KW - Thermostable esterase
UR - http://www.scopus.com/inward/record.url?scp=2942746205&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=2942746205&partnerID=8YFLogxK
U2 - 10.1016/j.femsle.2004.05.026
DO - 10.1016/j.femsle.2004.05.026
M3 - Article
C2 - 15212797
AN - SCOPUS:2942746205
SN - 0378-1097
VL - 236
SP - 97
EP - 102
JO - FEMS microbiology letters
JF - FEMS microbiology letters
IS - 1
ER -