Immobilization and characterization of porcine pancreas lipase

• Published in: Enzyme and microbial technology Vol. 20; no. 7; pp. 531 - 535
• Main Authors: Bagi, K., Simon, L.M., Szajáni, B.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier Inc 1997; Elsevier Science
• Subjects: Biological and medical sciences; Biotechnology; conformational stability; cross-linking; Fundamental and applied biological sciences. Psychology; immobilization; Immobilization of enzymes and other molecules; Immobilization techniques; Methods. Procedures. Technologies; Porcine pancreas lipase; Porcine pancreas lipase; conformational stability; immobilization; cross-linking; Temperature; Stability; Enzyme; Triacylglycerol lipase; Crosslinking; Esterases; Optimization; Carboxylic ester hydrolases; Characterization; Hydrolysis; Enzymatic activity; pH; Hydrolases; Immobilized enzyme
• ISSN: 0141-0229; 1879-0909
• DOI: 10.1016/S0141-0229(96)00190-1

Porcine pancreas lipase (triacylglycerol ester hydrolase, EC 3.1.1.3) was immobilized with the highest activity (2,187 U g −1 solid) on polyacrylamide beads possessing carboxylic functional groups activated by a water-soluble carbodiimide. The optimum pH for catalytic activity was pH 8.9. The apparent optimum temperature for the immobilized enzyme was about 7°C higher than that for the soluble enzyme. The immobilization stabilized the enzyme against heat and urea treatment. Cross-linking of the immobilized enzyme with glutaraldehyde or 3,5-difluoronitrobenzene improved the thermal stability. Application of the immobilized lipase for olive oil hydrolysis is also presented.