β-D-glucopyranosidase (βG, EC 3.2.1.21) is an enzyme of considerable importance in food technology for increasing the aroma of wines, musts, fruit juices and alcoholic beverages. In this research we have studied the stabilization of a commercial βG preparation, by covalent immobilization of its carbohydrate moiety to an amine agarose gel. The findings showed total adsorption of the enzyme, previously purified, on the matrix, its low reduction in activity and finally a high stabilization over time. β-d-glucopyranosidase (βG, EC 3.2.1.21) is an enzyme of considerable importance in food technology for increasing the aroma of wines, musts, fruit juices and alcoholic beverages. In this research we have studied the stabilization of a commercial βG preparation, by covalent immobilization of its carbohydrate moiety to an amine agarose gel. The findings showed total adsorption of the enzyme, previously purified [G. Spagna, D. Romagnoli, A. Martion, G. Bianchi, P.G. Pifferi, Enzyme Microb. Technol., 22 (1998) 298], on the matrix, its low reduction in activity and finally a high stabilization over time.
Stabilization of a β-glucosidase from Aspergillus niger by binding to an amine agarose gel
BARBAGALLO, Riccardo Nunzio;
2000-01-01
Abstract
β-D-glucopyranosidase (βG, EC 3.2.1.21) is an enzyme of considerable importance in food technology for increasing the aroma of wines, musts, fruit juices and alcoholic beverages. In this research we have studied the stabilization of a commercial βG preparation, by covalent immobilization of its carbohydrate moiety to an amine agarose gel. The findings showed total adsorption of the enzyme, previously purified, on the matrix, its low reduction in activity and finally a high stabilization over time. β-d-glucopyranosidase (βG, EC 3.2.1.21) is an enzyme of considerable importance in food technology for increasing the aroma of wines, musts, fruit juices and alcoholic beverages. In this research we have studied the stabilization of a commercial βG preparation, by covalent immobilization of its carbohydrate moiety to an amine agarose gel. The findings showed total adsorption of the enzyme, previously purified [G. Spagna, D. Romagnoli, A. Martion, G. Bianchi, P.G. Pifferi, Enzyme Microb. Technol., 22 (1998) 298], on the matrix, its low reduction in activity and finally a high stabilization over time.File | Dimensione | Formato | |
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Betaglucosidasi Aspergillus (2000).pdf
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