Soybean peroxidase was immobilized through its free aminogroups on glutaraldehyde-activated aminopropyl glass beads with controlled pore diameter in order to obtain a solid biocatalyst which could be reusable and biocompatible, as well as exploitable for industrial applications. In this communication, preliminary data about the chemical-physical and kinetic characterization of the immobilkized enzyme were reported.
Covalent immobilization of soybean peroxidase on aminopropyl glass beads
MARCHIS, TATIANA;CERRATO, Giuseppina;MAGNACCA, Giuliana;VISCARDI, Guido;LAURENTI, Enzo
2008-01-01
Abstract
Soybean peroxidase was immobilized through its free aminogroups on glutaraldehyde-activated aminopropyl glass beads with controlled pore diameter in order to obtain a solid biocatalyst which could be reusable and biocompatible, as well as exploitable for industrial applications. In this communication, preliminary data about the chemical-physical and kinetic characterization of the immobilkized enzyme were reported.
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