Lipase (EC.3.1.1.3) from Aspergillus carneus was purified 24-fold with 38% yield using hydrophobic interaction chromatography. The enzyme was a monomer glycolsylated to the extent of 12.3%. The N-terminal sequence of the lipase was serine-proline-threonine-phenylalanine-alanine and was different from most other reported lipases. The optimum pH and temperature were 9.0 and 37 degreesC, respectively. A. carneus lipase was stable in the pH range 8.0-10.0 for 24 h and at 70 degreesC for 5 min. It followed first order reaction kinetics during inactivation. It had a preference for lauric acid and 1,3-position specificity. The detergents, taurocholic acid, hexadecly trimethyl ammonium bromide and n-octyl-alpha-and n-octyl-beta-D-glucopyranosides strongly stimulated enzyme activity while SDS was a strong inhibitor. It showed high levels of activity in the presence of many organic solvents and Mg+ +, Na+ and NH4+ ions. Metal chelators had no effect on lipase activity while diethyl p-nitrophenyl phosphate and PMSF drastically inhibited. Thermostability and half-life of the lipase was enhanced by glycine, sorbitol, glycerol, glucose and ammonium chloride. The lyophilised enzyme retained its activity for more than 1 year at room temperature. (C) 2003 Elsevier Ltd. All rights reserved.