Next Article in Journal
Correction: Hashish et al. Development and Validation of a New TaqMan Real-Time PCR for the Detection of Ornithobacterium rhinotracheale. Microorganisms 2022, 10, 341
Previous Article in Journal
Diversity Patterns of Protists Are Highly Affected by Methods Disentangling Biological Variants: A Case Study in Oligotrich (s.l.) Ciliates
Previous Article in Special Issue
Synergy of Cellulase Systems between Acetivibrio thermocellus and Thermoclostridium stercorarium in Consolidated-Bioprocessing for Cellulosic Ethanol
 
 
Article

Reactivity of a Recombinant Esterase from Thermus thermophilus HB27 in Aqueous and Organic Media

1
Biochemistry Laboratory, CITACA-Agri-Food Research and Transfer Cluster, Campus Auga, Universidade de Vigo, 32004 Ourense, Spain
2
GalChimia, SA, Parque Empresarial de Touro, Parcelas 26-27, Fonte Díaz, 15822 Touro, Spain
3
Grupo EXPRELA, Centro de Investigacións Científicas Avanzadas (CICA), Facultade de Ciencias, Universidade da Coruña, 15071 A Coruña, Spain
*
Author to whom correspondence should be addressed.
Current address: International Iberian Nanotechnology Laboratory (INL), Avenida Mestre José Veiga, 4715 Braga, Portugal.
Current address: Chemical Food Safety Group, Nestlé Research, 1000 Lausanne, Switzerland.
Academic Editor: Juan M. Gonzalez
Microorganisms 2022, 10(5), 915; https://doi.org/10.3390/microorganisms10050915
Received: 2 March 2022 / Revised: 19 April 2022 / Accepted: 22 April 2022 / Published: 27 April 2022
(This article belongs to the Special Issue Novel Microbial Enzymes with Industrial Applications)
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. View Full-Text
Keywords: Thermus thermophilus; KLEST-3S; carboxylesterase; thermostability; enantioselectivity; interfacial activation Thermus thermophilus; KLEST-3S; carboxylesterase; thermostability; enantioselectivity; interfacial activation
Show Figures

Figure 1

MDPI and ACS Style

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

AMA Style

González-González R, Fuciños P, Beneventi E, López-López O, Pampín B, Rodríguez R, González-Siso MI, Cruces J, Rúa ML. Reactivity of a Recombinant Esterase from Thermus thermophilus HB27 in Aqueous and Organic Media. Microorganisms. 2022; 10(5):915. https://doi.org/10.3390/microorganisms10050915

Chicago/Turabian Style

González-González, Roberto, Pablo Fuciños, Elisa Beneventi, Olalla López-López, Begoña Pampín, Ramón Rodríguez, María Isabel González-Siso, Jacobo Cruces, and María Luisa Rúa. 2022. "Reactivity of a Recombinant Esterase from Thermus thermophilus HB27 in Aqueous and Organic Media" Microorganisms 10, no. 5: 915. https://doi.org/10.3390/microorganisms10050915

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop