Reactivity of a Recombinant Esterase from <i>Thermus thermophilus</i> HB27 in Aqueous and Organic Media
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 th...
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MDPI AG
2022-04-01
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| Series: | Microorganisms |
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| Online Access: | https://www.mdpi.com/2076-2607/10/5/915 |
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| author | Roberto González-González Pablo Fuciños Elisa Beneventi Olalla López-López Begoña Pampín Ramón Rodríguez María Isabel González-Siso Jacobo Cruces María Luisa Rúa |
| author_facet | Roberto González-González Pablo Fuciños Elisa Beneventi Olalla López-López Begoña Pampín Ramón Rodríguez María Isabel González-Siso Jacobo Cruces María Luisa Rúa |
| author_sort | Roberto González-González |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-10T03:22:52Z |
| format | Article |
| id | doaj.art-319120e55aef402d822f50d145f0c4b0 |
| institution | Directory Open Access Journal |
| issn | 2076-2607 |
| language | English |
| last_indexed | 2024-03-10T03:22:52Z |
| publishDate | 2022-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Microorganisms |
| spelling | doaj.art-319120e55aef402d822f50d145f0c4b02023-11-23T12:14:57ZengMDPI AGMicroorganisms2076-26072022-04-0110591510.3390/microorganisms10050915Reactivity of a Recombinant Esterase from <i>Thermus thermophilus</i> HB27 in Aqueous and Organic MediaRoberto González-González0Pablo Fuciños1Elisa Beneventi2Olalla López-López3Begoña Pampín4Ramón Rodríguez5María Isabel González-Siso6Jacobo Cruces7María Luisa Rúa8Biochemistry Laboratory, CITACA-Agri-Food Research and Transfer Cluster, Campus Auga, Universidade de Vigo, 32004 Ourense, SpainBiochemistry Laboratory, CITACA-Agri-Food Research and Transfer Cluster, Campus Auga, Universidade de Vigo, 32004 Ourense, SpainGalChimia, SA, Parque Empresarial de Touro, Parcelas 26-27, Fonte Díaz, 15822 Touro, SpainGrupo EXPRELA, Centro de Investigacións Científicas Avanzadas (CICA), Facultade de Ciencias, Universidade da Coruña, 15071 A Coruña, SpainGalChimia, SA, Parque Empresarial de Touro, Parcelas 26-27, Fonte Díaz, 15822 Touro, SpainGalChimia, SA, Parque Empresarial de Touro, Parcelas 26-27, Fonte Díaz, 15822 Touro, SpainGrupo EXPRELA, Centro de Investigacións Científicas Avanzadas (CICA), Facultade de Ciencias, Universidade da Coruña, 15071 A Coruña, SpainGalChimia, SA, Parque Empresarial de Touro, Parcelas 26-27, Fonte Díaz, 15822 Touro, SpainBiochemistry Laboratory, CITACA-Agri-Food Research and Transfer Cluster, Campus Auga, Universidade de Vigo, 32004 Ourense, SpainThe 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.https://www.mdpi.com/2076-2607/10/5/915<i>Thermus thermophilus</i>KLEST-3Scarboxylesterasethermostabilityenantioselectivityinterfacial activation |
| spellingShingle | Roberto González-González Pablo Fuciños Elisa Beneventi Olalla López-López Begoña Pampín Ramón Rodríguez María Isabel González-Siso Jacobo Cruces María Luisa Rúa Reactivity of a Recombinant Esterase from <i>Thermus thermophilus</i> HB27 in Aqueous and Organic Media Microorganisms <i>Thermus thermophilus</i> KLEST-3S carboxylesterase thermostability enantioselectivity interfacial activation |
| title | Reactivity of a Recombinant Esterase from <i>Thermus thermophilus</i> HB27 in Aqueous and Organic Media |
| title_full | Reactivity of a Recombinant Esterase from <i>Thermus thermophilus</i> HB27 in Aqueous and Organic Media |
| title_fullStr | Reactivity of a Recombinant Esterase from <i>Thermus thermophilus</i> HB27 in Aqueous and Organic Media |
| title_full_unstemmed | Reactivity of a Recombinant Esterase from <i>Thermus thermophilus</i> HB27 in Aqueous and Organic Media |
| title_short | Reactivity of a Recombinant Esterase from <i>Thermus thermophilus</i> HB27 in Aqueous and Organic Media |
| title_sort | reactivity of a recombinant esterase from i thermus thermophilus i hb27 in aqueous and organic media |
| topic | <i>Thermus thermophilus</i> KLEST-3S carboxylesterase thermostability enantioselectivity interfacial activation |
| url | https://www.mdpi.com/2076-2607/10/5/915 |
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