Abstract
The influence of key parameters in the kinetics of the transglycosylation system catalyzed by Aspergillus oryzae β-galactosidase when applied to the synthesis of galactosyl-ethylene glycol and galactosyl-glycerol has been studied. It was found that both acceptors were inhibitors of the enzyme, causing a decrease of 9 and 68 fold in enzyme catalytic efficiency in the presence of 4.0 M ethylene glycol and glycerol, respectively. The effect was characterized as “substrate-like inhibition”, suggesting the formation of a nonproductive enzyme-acceptor complex. Inhibition constants for both acceptors were determined as 618 mM for ethylene glycol and 244 mM for glycerol.
Acknowledgments
We thank Dr. V.M. Dee for linguistic revision of the manuscript.
Declaration of interest: The authors report no declarations of interest. The authors alone are responsible for the content and writing of the paper.
This work was supported by the “Programa de Desarrollo de las Ciencias Básicas” (PEDECIBA) and Project I+ D 408 funded by “Comisión Sectorial de Investigación Científica”, CSIC-UdelaR.