Biochemical studies on a versatile esterase that is most catalytically active with polyaromatic esters

Herein, we applied a community genomic approach using a naphthalene-enriched community (CN1) to isolate a versatile esterase (CN1E1) from the α/β-hydrolase family. The protein shares low-to-medium identity (≤ 57%) with known esterase/lipase-like proteins. The enzyme is most active at 25–30°C and pH ...

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Detalles Bibliográficos
Autores principales: Martínez-Martínez, Mónica, Lores, Iván, Peña-García, Carlina, Bargiela, Rafael, Reyes-Duarte, Dolores, Guazzaroni, María-Eugenia, Peláez, Ana Isabel, Sánchez, Jesús, Ferrer, Manuel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley & Sons Ltd 2014
Materias:
Brief Reports
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3937722/
https://www.ncbi.nlm.nih.gov/pubmed/24418210
http://dx.doi.org/10.1111/1751-7915.12107

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3937722/
https://www.ncbi.nlm.nih.gov/pubmed/24418210
http://dx.doi.org/10.1111/1751-7915.12107

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