Enzymatic transesterification for the synthesis of amino acid-sugar conjugates

Among the tested ten enzymes, Optimase M-440 showed the highest activity in transesterification of N-t-Boc-L-Phe-OTFE with D-glucose. Monosaccharides and their derivatives acted as good acyl acceptors in the Optimase M -440 catalyzed transesterification of N-t-Boc-L-Phe-OTFE. Optimase M-440 showed a preferable catalytic activity on the primary hydroxyl group of saccharides and a good regioselectivity. Optimase M-440 showed the highest activity in pyricline among the tested solvents. As acyl donors, trifluoroethyl esters of amino acids showed a high reactivity in transesterification. Optimase M-440 showed a broad substrate specificity towards amin 。 acid esters and saccharides.