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

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.
2nd EuCheMS Chemistry Congress: "Chemistry, The Global Science"
Torino
16-20/09/2008
Atti del 2nd EuCheMS Chemistry Congress: "Chemistry, The Global Science"
-
P046
P046
Marchis T.; Cerrato G.; Magnacca G.; Viscardi G.; Laurenti E.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2318/104868
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