Activity of magnetite-immobilized catalase in hydrogen peroxide decomposition

F. HORST; E. H. RUEDA; M. L. FERREIRA

ENZYME AND MICROBIAL TECHNOLOGY

Elsevier

Lugar: Amsterdam; Año: 2006 vol. 38 p. 1005 - 1012

0141-0229

Este trabajo fue aceptado el 31 de Agosto del 2005. Se publica en el volumen 38 (2006). The present work analyzes the activity in decomposition of H2O2 using magnetite-immobilized catalase. The support of catalase is a-glutaraldehyde treated magnetite (Fe3O4). The data obtained in the H2O2 decomposition are analyzed. The fitting of the initial rate of the H2O2 decomposition vs hydrogen peroxide concentration data is discussed using a specific program for enzyme kinetics modeling (LEONORA). The free catalase from Aspergillus niger (3, 5 or 10 U/mL) does not show substrate inactivation up to 0.4 M H2O2. The immobilized catalase at low catalyst concentration shows substrate inhibition. Using 1mg/mL of supported catalase the predicted maximum activity is higher than in the case of the free catalase at similar catalase concentration, although the optimum temperature is lower (40° vs 60° C).