| Summary: | The thermoalkalophilic membrane-associated esterase E34Tt from <i>Thermus thermophilus</i> HB27 was cloned and expressed in <i>Kluyveromyces lactis</i> (KLEST-3S esterase). The recombinant enzyme was tested as a biocatalyst in aqueous and organic media. It displayed a high thermal stability and was active in the presence of 10% (<i>v</i>/<i>v</i>) organic solvents and 1% (<i>w</i>/<i>v</i>) detergents. KLEST-3S hydrolysed triglycerides of various acyl chains, which is a rare characteristic among carboxylic ester hydrolases from extreme thermophiles, with maximum activity on tributyrin. It also displayed interfacial activation towards triacetin. KLEST-3S was also tested as a biocatalyst in organic media. The esterase provided high yields for the acetylation of alcohols. In addition, KLEST-3S catalyzed the stereoselective hydrolysis of (<i>R</i>,<i>S</i>)-ibuprofen methyl ester (87% ee). Our results indicate that KLEST-3S may be a robust and efficient biocatalyst for application in industrial bioconversions.
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