The transesterification of alpha-D-glucose with divinylsuccinate, divinyladipate and divinylsebacate in pyridine at 55degreesC for 3 days was catalyzed by an alkaline protease from Bacillus subtilis to give corresponding 6-O-vinyl glucose esters at 30%, 53% and 35% yield, respectively. The stereo-selectivity of the alkaline protease toward the alpha-anomer was affected by the acyl donor chain length. 6-O-Vinylsuccinyl-D-glucose was mixture of alpha- and beta-anomers (alpha/beta=44/56), the other two products were the pure alpha-D-glucose derivatives.