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Catecholase Experiment

Decent Essays

During this experiment, enzyme activity of catecholase and its relationships with enzyme concentration, pH, temperature, and substrate concentration were tested. Enzymes are proteins that speed up biochemical reactions. By using a spectrophotometer, absorbance rates of the various samples were measured and the enzyme activity for each relationship was observed. While we were testing the effects of enzyme concentration, we found that as the concentration of enzymes in solution increased, the higher the absorbance rate. We tested the absorbance of four samples, all containing different enzyme concentrations. When the relationship between enzyme concentration and absorbance is graphed, it shows a rapid increase that eventually levels out. …show more content…

This is because the reaction reaches maximum velocity, where the addition of more substrate would no longer affect absorbance because all of the enzymes are involved in the enzyme-substrate complex. When testing the affects of varying temperature, an inverse relationship was observed where increasing temperature decreased the reaction rate and absorbance. Three samples were placed in three different temperatures, 10°C, 24°C, and 50°C. After sitting for ten minutes, the absorbance of each sample was measured. Our results showed that optimal temperature was at 24°C. However, the actual ideal temperature was determined to be 10°C, where the absorbance is the highest. If the reaction is above or below the optimal temperature for that particular enzyme, the point where rate is maximized, then the rate decreases. At higher temperatures, some enzymes become denatured and will no longer function properly. The final relationship tested was enzyme activity and pH. Five samples with varying pHs were tested. After graphing, our data formed a bell-curve, where the optimal pH was recorded at seven. At any pH other than seven, the reaction rate decreased. Enzymes are sensitive to pH and will become denatured in environments

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