THE EFFECT OF DIFFERENT ACETATE BUFFER CONCENTRATIONS ON ENZYME ACTIVITY IN ELECTROCHEMICAL STUDIES

Abstract

In general, enzymes are soluble; They can be inhibited by various factors such as substrate, pH, buffer concentration and temperature. Optimum buffer concentration is an important factor for enzyme activity. Buffer solutions have a certain buffering capacity that is used to keep the pH of a system constant, which has only a small uncertainty. Buffer capacity is dependent on both concentration and pH. While buffer concentration is an important factor in electrochemical studies, this factor can be ignored in most studies. In this study, to determine the effect of buffer concentration on enzyme activity, the ionic strength effect of enzyme activity at different buffer concentrations was utilized by using cross-linked hydrogen peroxidase enzyme. It was prepared by immobilizing HRP enzyme, BSA, gelatin and glutaraldehyde on the gold electrode with the help of UV light. Measurements were made in 25, 50, 100 and 200 mM acetic acid buffer with electrodes prepared under the same conditions. In this study, it was aimed to emphasize that working at the right pH value is not sufficient, but also the importance of working at the right concentration. We can say that the concentration of the buffer to be used should be revealed by different studies that support the importance of enzyme performance