FATTY-ACID-MODIFIED ENZYMES AS ENANTIOSELECTIVE CATALYSTS IN MICROAQUEOUS ORGANIC MEDIA

Highly active lipase and protease complexes were prepared by non-coval ent modification with stearic acid. The protein content and yield of t he modified enzyme complexes depended on the enzymes' source. The incr ease in the transesterification activity of the modified enzymes was 1 5 fold for Candida rugosa lipase and porcine pancreatic lipase, with p reservation of the enantioselectivity. Pseudomonas sp. lipase which sh owed no activity in its crude form, exhibited an activity of 38 mu mol /h.mg protein in the modified form.