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Crystallization and preliminary X-ray crystallographic analysis of EstE1, a new and thermostable esterase cloned from a metagenomic library
EstE1, a new thermostable esterase, was isolated by functional screening of a metagenomic DNA library from thermal environment samples. This enzyme showed activity towards short-chain acyl derivatives of length C4–C6 at a temperature of 303–363 K and displayed a high thermostability above 353 K. Est...
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| Auteurs principaux: | , , , , |
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| Format: | Artigo |
| Langue: | Inglês |
| Publié: |
International Union of Crystallography
2006
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| Sujets: | |
| Accès en ligne: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2150951/ https://ncbi.nlm.nih.gov/pubmed/16511287 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1744309106000832 |
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