The P134Q Sucrose Phosphorylase: Subtle Changes in the Catalytic Properties Benefit the Production of 2-O-α-Glucosyl Glycerol.

ABSTRACT: Protein engineering of Bifidobacterium adolescentis sucrose phosphorylase (BaSucP) has previously identified the P134Q enzyme variant for site-selective glycosylation at the 2-OH of glycerol. Besides improvement in selectivity, the P134Q-BaSucP additionally involves enhanced affinity for glycerol as a biochemical property potentially important for the production of 2-O-α-glucosyl glycerol (2GG), a commercialized skincare ingredient for cosmetic applications. Here, we performed a detailed kinetic model-based evaluation of P134Q-BaSucP in initial-rate and full reaction time course analyses to obtain a mechanistic interpretation and a comprehensive assessment of the process improvements achievable by the P134Q variant compared to the native enzyme. We show that P134Q-BaSucP involves ∼50-fold

SUBMITTER: Sigg A 

PROVIDER: S-EPMC12322648 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature