Cargando…
Enhancing the thermostability of Rhizopus oryzae lipase by combined mutation of hot-spots and engineering a disulfide bond
Rhizopus oryzae lipase (ROL) is important because of its extreme sn-1,3-regioselectivity, but it shows poor thermostability, which severely restricts its application. In this work, the thermostability of ROL was greatly enhanced by rational design. First, several sites that may affect the thermostab...
Autores principales: | Zhao, Jiong-feng, Wang, Zhe, Gao, Fei-long, Lin, Jian-ping, Yang, Li-rong, Wu, Mian-bin |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society of Chemistry
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9091645/ https://www.ncbi.nlm.nih.gov/pubmed/35559271 http://dx.doi.org/10.1039/c8ra07767c |
Ejemplares similares
-
Engineering a Disulfide Bond in the Lid Hinge Region of Rhizopus chinensis Lipase: Increased Thermostability and Altered Acyl Chain Length Specificity
por: Yu, Xiao-Wei, et al.
Publicado: (2012) -
Enhanced thermostability of a Rhizopus chinensis lipase by in vivo recombination in Pichia pastoris
por: Yu, Xiao-Wei, et al.
Publicado: (2012) -
Identification of a hot-spot to enhance Candida rugosa lipase thermostability by rational design methods
por: Li, Guanlin, et al.
Publicado: (2018) -
Efficient production of (2)H, (13)C, (15)N-enriched industrial enzyme Rhizopus chinensis lipase with native disulfide bonds
por: Zhang, Meng, et al.
Publicado: (2016) -
Production of Rhizopus oryzae lipase using optimized Yarrowia lipolytica expression system
por: Vidal, Lea, et al.
Publicado: (2023)