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Improvement of the Thermostability and Activity of a Pectate Lyase by Single Amino Acid Substitutions, Using a Strategy Based on Melting-Temperature-Guided Sequence Alignment
In the vast number of random mutagenesis experiments that have targeted protein thermostability, single amino acid substitutions that increase the apparent melting temperature (T(m)) of the enzyme more than 1 to 2°C are rare and often require the creation of a large library of mutated genes. Here we...
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| Autors principals: | , , , , , , , , |
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| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
American Society for Microbiology (ASM)
2008
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2258563/ https://ncbi.nlm.nih.gov/pubmed/18156340 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/AEM.02220-07 |
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