LIPASE OF PENICILLIUM-CASEICOLUM

The lipase activity of Penicillium caseicolum was tested in a cell-free broth of the organism and in a partially purified preparation of the enzyme. The optimum reaction pH of the enzyme was 9.0 and the optimum temperature 35 °C. A mixture of CaCl2and sodium taurocholate enhanced the activity of the enzyme toward butter oil. The heat inactivation of this lipase was exponentially related to temperature. A z value of 16 °C and an inactivation energy of 32 200 cal/mol were calculated for this enzyme. Triglycerides of lower molecular weight fatty acids were better substrates than those of higher molecular weight fatty acids for this lipase. © 1990, American Chemical Society. All rights reserved.