Catalase is a common enzyme that is present in nearly all living organisms. Enzymes are proteins that catalyse selective chemical functions without altering the products or itself. In order to accelerate a reaction, the enzyme will bind to one or more reactant molecules known as the substrates. These substrates will bind to the enzyme’s selective active site, and will then be broken down into products. All chemical reactions that occur in a living organism depend on the actions of enzymes, and function in a temperate environment similar to the body temperature of a living organism. Each enzyme has particular conditions under which is functions optimally, and its activity can be altered by different factors. This includes the pH it is exposed …show more content…
The beginning reaction that occurred at the pH level of 1 shows that the mean reaction rate was incredibly low, at 2 mL/minute. This then increased by 57 units once it reached its peak productivity of 59 mL/minute observed at pH 8. pH levels 6, 7, and 8 only varied between 1 and 2 mL/minute, which demonstrated similar rates of reaction. At pH 10, the reaction rate decreased considerably as it declined by 58 mL/minute, and maintained that productivity at pH 12. The scatter graph included in the results section further solidify and visually represent these observations. The reaction rate of the catalase exposed to pH 1 is barely conceivable on the diagram as its average rate of reaction was 2 mL/minute. The graph shows that pH 3 grew exponentially compared to the previous, providing a mean rate of 54 mL/minute. The pH levels of 6, 7, and 8 provided the greatest rates of catalytic reaction, which can be clearly seen via the graph’s three highest peaks. These results were very similar, and provided reaction rates of 58, 57, and 59 mL/minute respectively. …show more content…
Because this pH was too acidic in comparison to its optimal range, the enzyme began to denture and was rendered inactive. As the pH grew closer to the optimal pH range, the reaction rates began to drastically increase, which is shown through the results provided from pH 3, 6, 7, and 8. However, pH 6, 7, and 8 were the most consecutively similar, and would therefore mean that the catalase optimum ranges from these three. From these levels, pH 8 provided the highest reaction rate of 59 mL/minute. From this data, it can be decided that this is the optimal level for the catalase. After this optimum is exceeded, the reaction rate sharply decreases to 1 mL/minute during pH 10 and 12. This reduction of activity can be explained through the act of denaturing. This occurs when the enzyme’s tertiary structure collapses, as the hydrogen bonds that form the protein begin to break apart. The function of proteins is heavily reliant on its structure, and once it deforms, it becomes ineffective. In this particular scenario, the active of the enzyme will alter and its once complementary substrate is unable to bind, preventing the reaction from