Determining The Effects Of PH, Temperature, Enzyme Concentration, And Substrate Concentration On The Activity Of Catacholase In Solanum Tuberosum

There are millions of living organisms that have important uses for enzymes as catalytic proteins. Enzymes increase reaction rate by lowering the activation energy of the reaction, however they are not consumed. An enzyme is present as both a reactant and a product in a reaction. Substrates are the reactants for an enzyme and since enzymes have such a high specificity, only specific substrates will fit on certain enzymes. These substrates bind to the active site of an enzyme and form enzyme-substrate complexes. Weak i

As shown in Figure 4, absorbance increases from pH 4 to pH7, and absorbance decreases from pH7 to pH 10. The highest absorbance is achieved at pH 7 therefore it would be the optimal pH level.

Five test tubes, to serve as blanks, were prepared. In each was placed 5ml of pH 7 phosphate buffer and 1ml of water. These tubes were labeled 10B, 20B, 30B, 40B, and 50B. Five more tubes were prepared similarly except instead of the water, 1ml of catechol was added. These tubes were labeled 10, 20, 30, 40, and 50. Tubes 10 and 10B were placed in the fridge, tubes 20 and 20B were left at room temperature, and the rest of the tubes were placed in their appropriate water baths. After 5 minutes, 1ml of the potato solution was added to each of the 10 tubes, they were mixed, and the tubes were left to sit in their treatments. At 1 minute intervals the tubes were mixed and after 5 minutes the absorbance of each tube was recorded at a wavelength of 420nm.

Experiment 1: Effect of Enzyme Concentration

As shown in Figure 2, increasing the concentration of 0.1% catechol increases the rate of benzoquinone formation, as shown by the increasing levels of absorbance. This trend is observable in all four substrate concentrations until the 4 minute mark. After 4 minutes graphs 3 and 4 begin to decrease in slope, which describes a leveling off of benzoquinone production. Furthermore, at 8 minutes graphs 3 and 4 decline slightly. Graphs 1 and 2 maintain a slightly more linear shape, which implies that their enzymatic reactions continue at a relatively steady pace throughout the experiment.

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Activity Five, Campbell Reece, , According Dixon, Enzyme Concentration, Dixon Webb, King Kozlov, Biekman Konietzny, Paul Gowda, Ancos Cano, phosphate buffer, substrate concentration, enzymatic activity, ph 7, optimal ph, reaction rate, 3 4, catechol added, added tube, enzyme substrate, catechol added tube, enzyme substrate concentration, temperature ph enzyme, graphs 3 4, ph enzyme substrate,