Improving the thermostability and modulating the inulin profile of inulosucrase through rational glycine-to-proline substitution.

The flexibility of protein structure plays a crucial role in enzyme stability and catalysis. Among the amino acids, glycine is particularly important in conferring flexibility to proteins. In this study, the effects of flexible glycine residues in 121 inulosucrase (LrInu) on stability and inulin profile were investigated through glycine-to-proline substitutions.

Energy- and evolution-based design of inulosucrase for enhanced thermostability and inulin production.

Inulosucrase from Lactobacillus reuteri 121 (LrInu) exhibits promise in the synthesis of prebiotic inulin and fructooligosaccharides. However, for its use in industry, LrInu's thermostability is a crucial consideration. In this study, the computational program FireProt was used to predict the thermostable variants of LrInu.