RT Journal Article
T1 Reactivity of a recombinant esterase from Thermus thermophilus HB27 in aqueous and organic media
A1 Gonzalez Gonzalez, Roberto
A1 Fuciños Gonzalez, Juan Pablo
A1 Beneventi, Elisa
A1 López López, Olalla
A1 Pampín, Begoña
A1 Rodríguez, Ramón
A1 González Siso, María Isabel
A1 Cruces, Jacobo
A1 Rua Rodriguez, María Luisa
K1 2302 Bioquímica
K1 3303.03 Procesos Químicos
K1 3303 Ingeniería y Tecnología Químicas
AB 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.
PB Microorganisms
SN 20762607
YR 2022
FD 2022-04-27
LK http://hdl.handle.net/11093/3438
UL http://hdl.handle.net/11093/3438
LA eng
NO Microorganisms, 10(5): 915 (2022)
NO Xunta de Galicia | Ref. 10MDS373027PR
DS Investigo
RD 20-sep-2024