HYDROGEN PEROXIDASE ENZYME ACTIVITY AT DIFFERENT CONCENTRATIONS OF BSA

Abstract

Cross-linked enzymes are more stable at a certain temperature than free enzymes. Bovine serum albumin (BSA), which has a large number of amine groups, provides a strong binding between enzyme aggregates, thus leading to increased activity and stability of the bioactive layer. The enzyme-BSA mixture becomes more stable after covalent bonding with a crosslinking agent such as glutaraldehyde. The HRP enzyme was immobilized on the gold electrode together with BSA, gelatin and glutaraldehyde with the help of UV light. Four different electrodes were prepared using different amounts of BSA at 7.5 mg, 15 mg, 30 mg and 60 mg concentrations for each electrode Using four different electrodes prepared, 16 electrochemical measurements were performed with four different ferrous iron analytes. Glutaraldehyde binds to the BSA polymer, which has a higher affinity than the enzyme, reducing the tight covalent cross-links caused by BSA on the HRP and ensuring the continuation of the enzyme activity. It was observed that different BSA concentrations significantly affected the enzyme activity. The concentration of polymers to be used for crosslinking enzymes is an important factor in electrochemical studies.