Immobilization of Bgps-Expressing Escherichia coli cells coated with ZIF-67 for the production of rare ginsenoside F1

Rare ginsenoside F1 is a potent medicinal component with low natural content. Currently, ginsenoside F1 is primarily produced through enzyme or microbial deglycosylation. Despite its high catalytic efficiency, biocatalyst reuse presents problems. Previously, we obtained ginsenoside hydrolase Bgps using gene mining and expressed it heterologously in E. coli. In this experiment, we immobilized Bgps-containing cells with ZIF-67 and used them for the synthesis of rare ginsenoside F1, thus solving the problem of poor reusability of free cells. Immobilized cells retained more than 80 % of the yield after five batches at 40 °C and pH 9.0 as compared to free cells, and their operational stability was significantly better. After 15 days at 4 °C, the immobilized cells preserved more than 70 % of their initial activity, remained stable, and showed good pH adaptation. This provides a green and sustainable method for the catalytic production of the rare ginsenoside F1 by immobilized cells.