Enzymatic synthesis of 2-aminoethyl β-d-galactopyranoside catalyzed by Aspergillus oryzae β-galactosidase

Glycosidases provide a powerful resource for in vitro synthesis of novel anomerically pure glycosides. Generation of new low molecular weight galactosides is of interest since they are potential galectin inhibitors. Galectins are molecular targets for cancer therapy and thus their inhibitors are potential antitumor agents. Here we report the enzymatic synthesis and structural characterization of 2-aminoethyl β-d-galactopyranoside. Critical parameters for transgalactosylation using either soluble or immobilized enzyme were investigated and optimized for the galactoside synthesis. We found that 0.2 M lactose, and 0.5 M 2-aminoethanol at 50 °C for 30 min were the optimal conditions for synthesis. 2-Aminoethanol proved to be an enzyme inhibitor, fitting a mixed inhibition model with inhibition constants, Kic = 0.31 ± 0.04 M and Kiu = 0.604 ± 0.035 M.

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► Enzymatic synthesis of aminoethyl β-d-galactopyranoside, was achieved.
► The success of the trasgalactosylation process depends on the reaction conditions.
► 2-Aminoethanol exerted enzyme inhibition following a mixed inhibition model.