This research presents progress made towards the development of an electrochemical biosensor to study the electrochemistry of the α-galactosidase enzyme, through immobilization of the enzyme upon the surface of various modified carbon paste electrodes (CPE’s). The ability to monitor concentrations of α-galactosidase is important because of the enzyme’s implications with regard to human health, as deficiency can result in the Lysosomal Storage Disorder Type II known as Fabry’s disease. The a-galactosidase enzyme was studied after immobilization to the surface of a variety of CPE’s, including plain CPE’s, as well as those chemically modified with 10% wt/wt palladium on activated charcoal and copper(II) phthalocyanine. The CPE’s fabricated were composed of graphite powder with mineral oil binder before the addition of the chemical modifiers. The sensitivity and selectivity of the CPE’s were characterized using cyclic voltammetry. Two methods of enzyme immobilization were used in this study. The first is a 10-minute immersion of the electrode surface in a 5% a-galactosidase solution. The second method involves attachment of the enzyme to the electrode surface by covalently bonding protein residues present in the enzyme to either amine or carboxylic acid functional groups attached to the surface of the electrode through an aryl diazonium salt reduction.

Electrochemistry of an α-galactosidase enzyme-immobilized modified carbon paste electrode biosensor

ACS Spring Meeting 2021

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.