Molecular Modification and Whole-cell Catalytic Optimization of Bifunctional Glutathione Synthase
GshF derived from Streptococcus thermophilus was expressed in Escherichia coli and site-directed mutagenesis was performed on GshFst to improve the enzyme activity and stability of GshF, and to optimize the whole-cell catalytic conditions of this mutant. Six different plasmids were tested to find the most suitable one, and then a one-factor test was used to optimize the induction conditions; on this basis, GshFst was modelled and molecularly docked using AlphaFold2, and the mutation sites were obtained by prediction. After single-site mutagenesis and combinatorial mutagenesis, the double mu
