Lipase-catalysed synthesis of glucose fatty acid esters in tert-butanol

Synthesis of 6-O-acylate-alpha-D-glycopyranose from underivatised substrate s in anhydrous tert-butanol was achieved using immobilised lipases from Can dida antarctica and Mucor miehei. Except for acetic acid, the initial react ion rates with the C. antarctica lipase were independent of acyl donor chai n lengths and in a range of 3.9 +/- 0.4 mu mol glucose converted min(-1) g enzyme preparation. The catalytic activity of the M. miehei lipase increase d with increasing acyl donor chain length with a maximum for stearic acid o f 0.45 mu mol min(-1) g. Using maltose as substrate, the catalytic activity decreased by a factor of 48 and 20 with the lipase from C. antarctica and M. miehei, respectively, while with maltotriose no reaction was observed.