Biochemical and Structural Characterization of a novel thermophilic esterase EstD11 provide catalytic insights for the HSL family

A novel esterase, EstD11, has been discovered in a hot spring metagenomic library. It is a thermophilic and thermostable esterase with an optimum temperature of 60°C. A detailed substrate preference analysis of EstD11 was done using a library of chromogenic ester substrate that revealed the broad su...

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Detalles Bibliográficos
Autores principales: Miguel-Ruano, Vega, Rivera, Ivanna, Rajkovic, Jelena, Knapik, Kamila, Torrado, Ana, Otero, José Manuel, Beneventi, Elisa, Becerra, Manuel, Sánchez-Costa, Mercedes, Hidalgo, Aurelio, Berenguer, José, González-Siso, María-Isabel, Cruces, Jacobo, Rúa, María L., Hermoso, Juan A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Research Network of Computational and Structural Biotechnology 2021
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7905190/
https://www.ncbi.nlm.nih.gov/pubmed/33680362
http://dx.doi.org/10.1016/j.csbj.2021.01.047

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7905190/
https://www.ncbi.nlm.nih.gov/pubmed/33680362
http://dx.doi.org/10.1016/j.csbj.2021.01.047

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