Immobilization and characterization of porcine pancreas lipase
Tipo de material:
TextoSeries ; Enzyme and Microbial Technology, 20(7), p.351-535, 1997Trabajos contenidos: - Bagi, K
- Simon, L. M
- Szajani, B
| Item type | Current library | Collection | Call number | Status | Date due | Barcode | |
|---|---|---|---|---|---|---|---|
Documentos solicitados
|
CICY Documento préstamo interbibliotecario | Ref1 | B-11141 (Browse shelf(Opens below)) | Available |
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.
There are no comments on this title.
