Heme protein-gluten films: voltammetric studies and their electrocatalytic properties

Abstract Direct electrochemistry and electrocatalysis of heme proteins, such as hemoglobin (Hb), myoglobin (Mb), and horseradish peroxidase (HRP), incorporated in gluten biopolymer films cast on pyrolytic graphite (PG) electrodes, were studied by voltammetry and amperometry. All the three protein-gluten films exhibited a pair of well-defined, quasi-reversible cyclic voltammetric peaks at about −0.28 V versus saturated calomel electrode (SCE) in pH 5.5 buffers, respectively, characteristic of the heme Fe(III)/Fe(II) redox couples, indicating enhanced electron transfer between the proteins and PG electrodes in a gluten film environment. The protein-gluten hydrogel films showed excellent stability. Positions of Soret absorption band of protein-gluten films suggested that the heme proteins kept their secondary structure similar to their native state in the films in the medium pH range. The heme proteins in gluten films were act as a biologic catalyst to catalyze reduction of oxygen or hydrogen peroxide. The voltammetric or amperometric responses of H 2 O 2 at the protein-gluten film electrodes could be used to determine the concentration of H 2 O 2 in solution.

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