As shown in Figure 1, the sample containing 2 ml of the enzyme had the greatest rate of absorbance change (m= 0.007) when mixed with substrate and dye (Figure 1), indicating that the substrate was being converted to product faster than the samples that contained 0.5 ml and 1 ml of enzyme. The second experiment included the measurement of temperature effects on Catalase. The results varied for each temperature used. The optimal temperature for this enzyme was forty-eight degrees Celsius. The enzyme’s temperature continued to increase at this temperature. During the experiment, the enzyme at seven degrees had an increase in temperature, while at sixty degrees remained stagnant. The zero degrees and one hundred degrees reaction rates are similar …show more content…
The third and final experiment included a measure of pH effects on Catalase. Based on the graph below, (Figure 3), the optimal pH for the enzyme was a pH level of five. The slope of the pH level five is the highest and the reaction at this level increased the most in comparison to the others. The slope of this pH was 0.0081. pH levels at the extreme end of the pH scale will denature the shape of the enzyme and will not allow it to function properly. The pH at level three was stagnant and at pH level nine there was slight activity in this experiment as displayed in Figure 3 below. Figure 3: pH effects on …show more content…
If the temperature is far from the optimal temperature the enzyme reaction slows down or cannot work at all. If the conditions are outside the normal range, the Catalase loses the ability to catalyze the peroxide reaction. Once Catalase loses this ability, some of the chemical bonds of the enzyme capitulate and the enzyme’s three-dimensional structure begins to decompose, and the enzyme begins to denature. As the temperature rises, reacting molecules increase the kinetic energy. This increases the chances of a positive collision and the rate