Sucrose phosphorylase from Lactobacillus reuteri: Characterization and application of enzyme for production of 2-O-α-d-glucopyranosyl glycerol.

The enzymatic synthesis of 2-O-α-d-glucopyranosyl-glycerol (2-αGG) by transglycosylation activity of sucrose phosphorylase (SPase) is a promising method for 2-αGG manufacturing. However, there are only a few SPases available for 2-αGG production. Here, we report on the characterization and application of SPase from Lactobacillus reuteri (LrSPase).

Synthesis of a series of validoxylamine A esters and their biological activities.

Background: The worldwide reduction in food production due to pests and diseases is still an important challenge facing today. Validoxylamine A (VAA) is a natural polyhydroxyl compound derived from validamycin, acting as an efficient trehalase inhibitor with insecticidal and antifungal activities. To extend the application and discover green pesticide, a series of ester derivatives were prepared based on VAA as a lead compound.

[Application of sucrose phosphorylase in glycosylation].

Water solubility, stability, and bioavailability, can be substantially improved after glycosylation. Glycosylation of bioactive compounds catalyzed by glycoside hydrolases (GHs) and glycosyltransferases (GTs) has become a research hotspot. Thanks to their rich sources and use of cheap glycosyl donors, GHs are advantageous in terms of scaled catalysis compared to GTs.

Insight into the glycosylation and hydrolysis kinetics of alpha-glucosidase in the synthesis of glycosides.

α-Glucosidase, Agl2, from Xanthomonas campestris was successfully overexpressed in Escherichia coli BL21(DE3) cells and purified with Ni columns. The enzyme exhibits glycosylation abilities towards a wide range of phenolic substrates, including phenol, vanillin, and ethyl vanillin, with maltose as the glycosyl donor. The catalytic properties of the purified enzyme were further investigated.