Reactivity of a Recombinant Esterase from Thermus thermophilus HB27 in Aqueous and Organic Media
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Reactivity of a Recombinant Esterase from Thermus thermophilus HB27 in Aqueous and Organic MediaAuthor(s)
Date
2022-04-27Citation
González-González, R.; Fuciños, P.; Beneventi, E.; López-López, O.; Pampín, B.; Rodríguez, R.; González-Siso, M.I.; Cruces, J.; Rúa, M.L. Reactivity of a Recombinant Esterase from Thermus thermophilus HB27 in Aqueous and Organic Media. Microorganisms 2022, 10, 915. https://doi.org/10.3390/microorganisms10050915
Abstract
[Abstract] The thermoalkalophilic membrane-associated esterase E34Tt from Thermus thermophilus HB27 was cloned and expressed in Kluyveromyces lactis (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% (v/v) organic solvents and 1% (w/v) 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 (R,S)-ibuprofen methyl ester (87% ee). Our results indicate that KLEST-3S may be a robust and efficient biocatalyst for application in industrial bioconversions.
Keywords
Thermus thermophilus
KLEST-3S
Carboxylesterase
Thermostability
Enantioselectivity
Interfacial activation
KLEST-3S
Carboxylesterase
Thermostability
Enantioselectivity
Interfacial activation
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Rights
Atribución 4.0 Internacional
ISSN
2076-2607