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

Yoichi Suzuki, Kenji Miyamoto, Hiromichi Ohta

Research output: Contribution to journalArticlepeer-review

38 Citations (Scopus)

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°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.

Original languageEnglish
Pages (from-to)97-102
Number of pages6
JournalFEMS microbiology letters
Volume236
Issue number1
DOIs
Publication statusPublished - 2004 Jul 1

Keywords

  • Archaeon
  • Recombinant fusion protein
  • Sulfolobus tokodaii
  • Thermostable esterase

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology
  • Genetics

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