This paper reports the electrochemical behaviour, relative to the Fe(III)-Fe(II) conversion, of horseradish peroxidase (HRP) entrapped within a solid matrix, at a pyrolytic graphite electrode. The results indicate that (i) immobilization enhances the electron exchange between the protein and the electrode surface; (ii) reversible electron transfer (eT) is achieved within a wide pH range (pH 3.0-12.0) even in the absence of mediators, (ii) the embedded protein shows native-like structural properties and increased stability. The results obtained may be of potential value, since they represent a first step for engineering a novel 'solid-state' electrode system, of importance for basic and applied biochemistry.This paper reports the electrochemical behaviour, relative to the Fe(III)-Fe(II) conversion, of horseradish peroxidase (HRP) entrapped within a solid matrix, at a pyrolytic graphite electrode. The results indicate that (i) immobilization enhances the electron exchange between the protein and the electrode surface; (ii) reversible electron transfer (eT) is achieved within a wide pH range (pH 3.0-12.0) even in the absence of mediators, (ii) the embedded protein shows native-like structural properties and increased stability. The results obtained may be of potential value, since they represent a first step for engineering a novel `solid-state' electrode system, of importance for basic and applied biochemistry.
Ferri, T., Poscia, A., Santucci, R. (1998). Direct electrochemistry of membrane-entrapped horseradish peroxidase. Part I. A voltammetric and spectroscopic study. BIOELECTROCHEMISTRY AND BIOENERGETICS, 44(2), 177-181 [10.1016/S0302-4598(97)00088-3].
Direct electrochemistry of membrane-entrapped horseradish peroxidase. Part I. A voltammetric and spectroscopic study
SANTUCCI, ROBERTO
1998-01-01
Abstract
This paper reports the electrochemical behaviour, relative to the Fe(III)-Fe(II) conversion, of horseradish peroxidase (HRP) entrapped within a solid matrix, at a pyrolytic graphite electrode. The results indicate that (i) immobilization enhances the electron exchange between the protein and the electrode surface; (ii) reversible electron transfer (eT) is achieved within a wide pH range (pH 3.0-12.0) even in the absence of mediators, (ii) the embedded protein shows native-like structural properties and increased stability. The results obtained may be of potential value, since they represent a first step for engineering a novel 'solid-state' electrode system, of importance for basic and applied biochemistry.This paper reports the electrochemical behaviour, relative to the Fe(III)-Fe(II) conversion, of horseradish peroxidase (HRP) entrapped within a solid matrix, at a pyrolytic graphite electrode. The results indicate that (i) immobilization enhances the electron exchange between the protein and the electrode surface; (ii) reversible electron transfer (eT) is achieved within a wide pH range (pH 3.0-12.0) even in the absence of mediators, (ii) the embedded protein shows native-like structural properties and increased stability. The results obtained may be of potential value, since they represent a first step for engineering a novel `solid-state' electrode system, of importance for basic and applied biochemistry.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
