Bio Lab - Analysis of the Enzyme Alkaline Phosphate and its...

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Analysis of the Enzyme Alkaline Phosphate and its Activity under Conditions of Varying pH, Substrate Concentration, Enzyme Concentration, Temperature, and with Inhibitors Abstract The purpose of our study was to find optimal ranges of temperature, substrate concentration, enzyme concentration and pH for our enzyme. The enzyme alkaline phosphate was used in our study. First we tested to see the enzyme rate of reaction with various inhibitors. The inhibitors included potassium molybdate, inorganic phosphate, and phenyl phosphate. All of these inhibitors slowed down the rate of reaction. A complete solution without inhibitors had a rate of .457 absorbance over 10 minutes. When the molybdate was added the rate went down to .257 absorbance over 10 minutes. When the inorganic phosphate was added the reaction rate went down to .086 absorbance over 10 minutes. When the phenyl phosphate was added the rate went down to .286 absorbance over 10 minutes. We found that certain inhibitors acted more aggressively than others, particularly inorganic phosphate. We then tested the effects of the enzyme concentration from a dilution of 1 mL to .0625 mL. We found that the rate of reaction decreased as the enzyme concentration decreased which leads us to believe that an optimal enzyme concentration would be very high. We also tested substrate concentration from .4 mM to .025 mM. We saw that even with a high substrate concentration the enzymatic activity was greater than that of a low substrate concentration. In our study of pH from 4 to 12 we saw that a pH level of 10 was the optimal level. For temperature, we found that 37 degrees centigrade was optimal for the enzyme. We tested ranges from 0 degrees to 100 degrees. From this we have concluded that the enzymes optimal level of activity includes a pH of 10 with a
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temperature of 37 degrees centigrade with high levels of enzyme and substrate concentration and with no inhibitors. Introduction Enzymes are biological catalysts that increase the speed of a chemical reaction by lowering the activation energy (Solomon et al., 2008). A substrate is the substance which an enzyme acts (Solomon et al., 2008). The enzyme and substrate come together to from the ES complex which then catalyzes the reaction and a product is formed (Solomon et al., 2008). Enzymes generally work best under certain conditions such as appropriate temperature, pH, and ion concentration (Solomon et al., 2008). An inhibitor decreases the rate of the enzymatic reaction (Solomon et al., 2008). Our study is to find the optimal situations for the enzyme alkaline phosphate to work. We would like the enzyme to help catalyze the reaction of pNPP into PnP+Pi and we will find the optimal ranges of pH, temperature, substrate and enzyme
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This note was uploaded on 04/04/2008 for the course BME 125 taught by Professor Bme during the Spring '08 term at Rutgers.

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Bio Lab - Analysis of the Enzyme Alkaline Phosphate and its...

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