Testing temperature and pH stability of the catalase enzyme in the presence of inhibitors

Abstract

The catalase enzyme is analyzed under different conditions in order to get a better understanding of its function, purpose and benefit to organisms. This enzyme resides in all living organisms that have exposure to oxygen. It uses hydrogen peroxide (H2O2) as its substrate, and is responsible for breaking down H2O2 into oxygen and water, therefore neutralizing oxidative stress in the cells. Maintaining the levels of oxidative stress is highly important because of the impact that the reactive oxidative species (ROS) have on the cells. ROS damage cells by targeting DNA and proteins leading to various complications and illnesses such as cancer, diabetes, neurodegenerative diseases and they even have an impact on the process of aging. To determine the activity of the catalase enzyme and test its stability, different temperatures and pH were employed, along with examining the catalase behavior under the presence of ascorbic acid as an inhibitor. Three samples were used for this experiment: animal sample, plant sample and microorganisms. The indicator of the reaction which aided in the process of determining whether catalase is performing its function was the formation of gas bubbles in the test tubes, and the quantity of that indicator assisted in drawing conclusions about the enzyme activity. This study revealed that the optimum conditions for catalase enzyme activity tend to be 37 °C at a pH of 7, especially present in liver and yeast samples. Ascorbic acid has proven to be a valuable inhibitor of the catalase enzyme. Extremely high or low temperature, along with highly acidic or basic environments tend to alter the enzyme activity disallowing it to perform its key role.