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Cumulative Effect of Amino Acid Replacements Results in Enhanced Thermostability of Potato Type L α-Glucan Phosphorylase
The thermostability of potato type L α-glucan phosphorylase (EC 2.4.1.1) was enhanced by random and site-directed mutagenesis. We obtained three single-residue mutations—Phe39→Leu (F39L), Asn135→Ser (N135S), and Thr706→Ile (T706I)—by random mutagenesis. Although the wild-type enzyme was completely i...
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| Główni autorzy: | , , , , |
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| Format: | Artigo |
| Język: | Inglês |
| Wydane: |
American Society for Microbiology
2005
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| Hasła przedmiotowe: | |
| Dostęp online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1214682/ https://ncbi.nlm.nih.gov/pubmed/16151135 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/AEM.71.9.5433-5439.2005 |
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