A purified alkaline thermotolerant bacterial lipase from Bacillus coagidans BTS-3 was immobilized on nylon-6 matrix activated by glutaraldehyde. The matrix showed similar to 70% binding efficiency for lipase. The bound lipase was used to perform transesterification in n-heptane. The reaction studied was conversion of vinyl acetate and butanol to butyl acetate and vinyl alcohol. Synthesis of butyl acetate was used as a parameter to study the transesterification reaction. The immobilized enzyme achieved similar to 75% conversion of vinyl acetate and butanol (100 mmol/L each) into butyl acetate in n-heptane at 55 degrees C in 12 h. When alkane of C-chain lower or higher than n-heptane was used as an organic solvent, the conversion of vinyl acetate and butanol to butyl acetate decreased. During the repetitive transesterification under optimal conditions, the nylon bound lipase produced 77.6 mmol/L of butyl acetate after third cycle of reuse. (c) 2007 Wiley Periodicals, Inc.