info:eu-repo/semantics/article
Immobilization of catalase from Aspergillus niger on inorganic and biopolymeric supports for H2O2 decomposition
Fecha
2004-02Registro en:
Eberhardt, Andrea Mariel; Pedroni, Viviana Isabel; Volpe, María Alicia; Ferreira, María Luján; Immobilization of catalase from Aspergillus niger on inorganic and biopolymeric supports for H2O2 decomposition; Elsevier Science; Applied Catalysis B: Environmental; 47; 3; 2-2004; 153-163
0926-3373
CONICET Digital
CONICET
Autor
Eberhardt, Andrea Mariel
Pedroni, Viviana Isabel
Volpe, María Alicia
Ferreira, María Luján
Resumen
This paper studies the H2O2 decomposition using supported catalase. The supports are γ-Al2O3, FeCl2-treated γ-Al2O3, glutaraldehyde-treated chitosan and glutaraldehyde-treated cellulose. Catalase/γ-Al2O3 is inactive, but the treatment with FeCl2 renders the oxide active. The extended Hückel type analysis (EHMO) indicates that the alumina-catalase interaction is strong, suggesting that a denaturation of the enzyme is accomplished when supporting on this oxide. Amongst all the samples, catalase/glutaraldehyde-cellulose is the most active, especially after 6 months of storage. After aging, catalase/glutaraldehyde-chitosan becomes inactive, probably due to the fact that NH2 groups on chitosan react with the enzyme active sites.