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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 ...
| Autores principales: | , , , , , , , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
John Wiley & Sons Ltd
2014
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| Materias: | |
| 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 |