Immobilization and characterization of porcine pancreas lipase
Immobilization and characterization of porcine pancreas lipase
- Enzyme and Microbial Technology, 20(7), p.351-535, 1997 .
Porcine pancreas lipase (triacylglycerol ester hydrolase, EC 3.1.1.3)was immobilized with the highest activity (2,187 U g-t solid)on polyactylamide beads possessing carboxylic functional groups activated by a watersoluble 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.
PORCINE PANCREAS LIPASE
IMMOBILIZATION
CROSS-LINKING
CONFORMATIONAL STABILITY
Porcine pancreas lipase (triacylglycerol ester hydrolase, EC 3.1.1.3)was immobilized with the highest activity (2,187 U g-t solid)on polyactylamide beads possessing carboxylic functional groups activated by a watersoluble 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.
PORCINE PANCREAS LIPASE
IMMOBILIZATION
CROSS-LINKING
CONFORMATIONAL STABILITY