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- W4361304212 abstract "L-arabinose isomerase (L-AI) is the key enzyme that isomerizes D-galactose to D-tagatose. In this study, to improve the activity of L-arabinose isomerase on D-galactose and its conversion rate in biotransformation, an L-arabinose isomerase from Lactobacillus fermentum CGMCC2921 was recombinantly expressed and applied in biotransformation. Moreover, its substrate binding pocket was rationally designed to improve the affinity and catalytic activity on D-galactose. We show that the conversion of D-galactose by variant F279I was increased 1.4 times that of the wild-type enzyme. The Km and kcat values of the double mutant M185A/F279I obtained by superimposed mutation were 530.8 mmol/L and 19.9 s-1, respectively, and the catalytic efficiency was increased 8.2 times that of the wild type. When 400 g/L lactose was used as the substrate, the conversion rate of M185A/F279I reached a high level of 22.8%, which shows great application potential for the enzymatic production of tagatose from lactose." @default.
- W4361304212 created "2023-03-31" @default.
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- W4361304212 date "2023-03-25" @default.
- W4361304212 modified "2023-09-24" @default.
- W4361304212 title "[Rational design of L-arabinose isomerase from Lactobacillus fermentum and its application in D-tagatose production]." @default.
- W4361304212 doi "https://doi.org/10.13345/j.cjb.220805" @default.
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