تحميل...
Improving low-temperature activity and thermostability of exo-inulinase InuAGN25 on the basis of increasing rigidity of the terminus and flexibility of the catalytic domain
Enzymes displaying high activity at low temperatures and good thermostability are attracting attention in many studies. However, improving low-temperature activity along with the thermostability of enzymes remains challenging. In this study, the mutant Mut8S, including eight sites (N61E, K156R, P236...
محفوظ في:
| الحاوية / القاعدة: | Bioengineered |
|---|---|
| المؤلفون الرئيسيون: | , , , , , , , |
| التنسيق: | Artigo |
| اللغة: | Inglês |
| منشور في: |
Taylor & Francis
2020
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| الموضوعات: | |
| الوصول للمادة أونلاين: | https://ncbi.nlm.nih.gov/pmc/articles/PMC8291790/ https://ncbi.nlm.nih.gov/pubmed/33131413 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1080/21655979.2020.1837476 |
| الوسوم: |
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