IMMOBILIZATION AND CHARACTERIZATION OF PORCINE PANCREAS LIPASE

Porcine pancreas lipase (triacylglycerol ester hydrolase, EC 3.1.1.3) was immobilized with the highest activity (2,187 U g(-1) solid) on pol yacrylamide beads possessing carboxylic functional groups activated by a water-soluble carbodiimide. The optimum pH for catalytic activity w as pH 8.9. The apparent optimum temperature for the immobilized enzyme was about 7 degrees C higher than that for the soluble enzyme. The im mobilization stabilized the enzyme against heat and urea treatment. Cr oss-linking of the immobilized enzyme with glutaraldehyde or 3,5-diflu oronitrobenzene improved the thermal stability. Application of the imm obilized lipase for olive oil hydrolysis is also presented. (C) 1997 b y Elsevier Science Inc.