| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10544024 | Food Chemistry | 2005 | 4 Pages |
Abstract
A commercial inulinase preparation immobilized on various supports was used for sucrose hydrolysis. Entrapment and encapsulation in Ca-alginate and entrapment in an alginate-silicate sol-gel matrix were evaluated. Best results were obtained with Ca-alginate beads. The influence of sodium-alginate concentration on the immobilization yield was assessed. Inulinase entrapped in Ca-alginate beads displayed high activity in the range 50-60 °C, whereas the optimum for the free enzyme was 60 °C. The optimum pH of the immobilized enzyme was slightly more acidic (4.0) than the one observed for the free form (4.5). The apparent KM for sucrose of the immobilized inulinase was 184 mM, as compared to 82 mM for free inulinase, as a result of diffusion resistances.
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Authors
R. Catana, B.S. Ferreira, J.M.S. Cabral, P. Fernandes,