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...

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Detalles Bibliográficos
Autores principales: Zhang, Rui, He, Limei, Shen, Jidong, Miao, Ying, Tang, Xianghua, Wu, Qian, Zhou, Junpei, Huang, Zunxi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2020
Materias:
Research Paper
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8291790/
https://www.ncbi.nlm.nih.gov/pubmed/33131413
http://dx.doi.org/10.1080/21655979.2020.1837476

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8291790/
https://www.ncbi.nlm.nih.gov/pubmed/33131413
http://dx.doi.org/10.1080/21655979.2020.1837476

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