Abstract
Horseradish peroxidase (EC 1.11.1.7) was immobilized on a polytryptophan film by (i) covalent coupling and by (ii) glutaraldehyde cross-linking. Covalent coupling was done by (i) carbodiimide on an activated bare electrode and also by (ii) glutaraldehyde coupling to a polytryptophan film. The polytryptophan film was formed by electropolymerization of tryptophan from acid solution (H 2SO 4) with a cross-linker (spermine). The film formed was electrically conducting, as proven by impedance studies. The enzyme can be coupled to this film by covalent coupling with glutaraldehyde. Impedance studies and cyclic voltammetric studies of this electrode suggest that the film may be useful in a variety of applications.
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