Redesign of a novel d-allulose 3-epimerase from Staphylococcus aureus for thermostability and efficient biocatalytic production of d-allulose

Abstract Background A novel d-allulose 3-epimerase from Staphylococcus aureus (SaDAE) has been screened as a d-allulose 3-epimerase family enzyme based on its high specificity for d-allulose. It usually converts both d-fructose and d-tagatose to respectively d-allulose and d-sorbose. We targeted pot...

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Hlavní autoři: Zhangliang Zhu, Dengke Gao, Chao Li, Ying Chen, Menglu Zhu, Xin Liu, Masaru Tanokura, Hui-Min Qin, Fuping Lu
Médium: Artigo
Jazyk:Inglês
Vydáno: BMC 2019-03-01
Edice:Microbial Cell Factories
Témata:
d-Allulose 3-epimerase
Structural analysis
TIM-barrel fold
Site-directed saturation mutagenesis
Thermostability
On-line přístup:http://link.springer.com/article/10.1186/s12934-019-1107-z
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