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EFFECTS OF TEMPERATURE, PH, AND SUBSTRATE INHIBITORS OF VARIOUS CONCENTRATIONS ON THE RATE OF ENZYME- CATALYZED REACTIONS USING ALKALINE PHOSPHATASE ABSTRACT The enzyme, alkaline phosphatase’s effects were assayed at pH levels ranging from 4.0 to 12.0 and with temperatures ranging from 0 o C to 100 o C. The enzyme was also studied using the substrate inhibitors molybdate, inorganic phosphate, and phenyl phosphonateon. All three acted as inhibitors, decreasing the reaction rate. When the concentration of the enzyme and substrate increases, the enzyme activity is at a pH of 7. The results found that inorganic phosphate proved to be the best inhibitor and phenyl phosphonate to be the worst inhibitor. The results showed that the optimal pH for the enzyme was 10.0 and absorbed best at a temperature of 100 o C. The experiments show that inhibitors, substrate concentration, pH and temperature affect the reaction rate of the enzyme alkaline phosphatase. INTRODUCTION Enzymes are complex proteins produced by all living organisms. They are vital biological molecules made by the cell in order to regulate certain biochemical reactions (Solomon et al., 2008). Enzymes speed up the reaction time by lowering the activation energy of a specific reaction (Solomon et al., 2008). Enzymes act upon substrates, and the product is the resulting
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substance of the reaction. To determine optimal conditions for enzyme activity, factors such as pH, temperature, and substrate inhibitors must be carefully considered. Alkaline phosphatase, the enzyme experimented on in this lab, is essential in removing phosphate groups from biological molecules such as alkaloids, proteins, and nucleotides (Solomon et al., 2008). In the experiment, molybdate, inorganic phosphate, and phenyl phosphonate were all used to represent substrate inhibitors. Substrate inhibitors block the enzyme from the substrate; in this lab pNPP was the substrate. The result of alkaline phosphatase combining with the substrate leads to the product pNP + P i . We predicted that the presence of sodium molybdate would act as a non-competitive inhibitor, altering the active site’s shape and form. We also predicted that phenyl phosphonate would act as an active inhibitor; phenyl phosponate would bind to the active site of the enzyme. Finally, we predicted that inorganic phosphate would decrease the rate of reaction by causing an
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This note was uploaded on 03/02/2009 for the course BIO 101 taught by Professor Martin during the Fall '08 term at Rutgers.

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