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Immobilization and characterization of porcine pancreas lipase

Tipo de material: TextoTextoSeries ; Enzyme and Microbial Technology, 20(7), p.351-535, 1997Trabajos contenidos:
  • Bagi, K
  • Simon, L. M
  • Szajani, B
Tema(s): Recursos en línea: Resumen: 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.
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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.

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