Most biochemical reactions are catalyzed by enzymes. Without enzymes, most reactions necessary for the maintenance of life would occur so slow that they would not occur at all under the regular temperature and pressure conditions (Cooper). Enzymes act as catalysts that accelerate the rates of reactions by lowering the energy of activation. In an enzymatic reaction, the substrate (which is the reactant that an enzyme acts on) binds to the active site (which is the region on the enzyme where the substrate binds to) of the enzyme (Reece). The catalysis of a reaction with enzyme proceeds in the following manner: Enzyme + Substrate <-> Enzyme-Substrate Complex <-> Enzyme + Product (Reece). Note that the enzyme is unaltered in the reaction and can
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Substrates bind to the active sites using hydrogen bonds, hydrophobic interactions, and ionic bonds. After the binding, the configurations of both the enzyme and substrate change to make an induced fit for the enzyme-substrate complex, and the enzyme uses different mechanisms to convert the substrate to a product (therefore releasing energy) and then release it from active site, which opens up for another substrate (specific to that active site only) to bind to it, starting the process over again. Environmental conditions that affect the activity of enzymes include pH levels, temperature, and concentration of the enzyme or the product (Sols). In this experiment, we are exploring how the varying concentrations of enzymes and products have on the activity of the enzyme Alkaline Phosphatase while using the substrate P-Nitrophenyl phosphate. In class, we learn that increasing the concentration of either enzyme or substrate will help increase the reaction rate. However, after a certain point, any increased concentration will not have any effect on the rates because there are more of one substance (either enzyme or substrate) than the other (Factors affecting Enzyme …show more content…
In Part C, two samples were tested for the concentration of products, one sample with enzyme and one sample without. The following parts consisted first of varying concentrations of the enzyme were used, while leaving the substrate concentration constant and second, varying concentrations of substrate were used, while leaving the enzyme concentrations constant to gather absorbance values. The data were then graphed in the following manner: the enzyme concentrations were plotted against time in one-minute intervals over the course of 10 minutes. The rate of reactions (velocities) and enzyme activities were calculated in order to be used to analyze the reactivity of the enzyme and substrates. For Part B, students made five dilution solutions having the following concentrations respectively: 0.0025mM, 0.005mM, 0.01mM, 0.025mM, 0.05mM and then they were inserted into the spectrophotometer, which was first blanked using a “blank” sample containing sodium bicarbonate buffer, to obtain the absorbance values. The data were then graphed (Concentration (mM) on the x-axis and absorbance on the y-axis) to obtain a standard
Substrates bind to the active sites using hydrogen bonds, hydrophobic interactions, and ionic bonds. After the binding, the configurations of both the enzyme and substrate change to make an induced fit for the enzyme-substrate complex, and the enzyme uses different mechanisms to convert the substrate to a product (therefore releasing energy) and then release it from active site, which opens up for another substrate (specific to that active site only) to bind to it, starting the process over again. Environmental conditions that affect the activity of enzymes include pH levels, temperature, and concentration of the enzyme or the product (Sols). In this experiment, we are exploring how the varying concentrations of enzymes and products have on the activity of the enzyme Alkaline Phosphatase while using the substrate P-Nitrophenyl phosphate. In class, we learn that increasing the concentration of either enzyme or substrate will help increase the reaction rate. However, after a certain point, any increased concentration will not have any effect on the rates because there are more of one substance (either enzyme or substrate) than the other (Factors affecting Enzyme …show more content…
In Part C, two samples were tested for the concentration of products, one sample with enzyme and one sample without. The following parts consisted first of varying concentrations of the enzyme were used, while leaving the substrate concentration constant and second, varying concentrations of substrate were used, while leaving the enzyme concentrations constant to gather absorbance values. The data were then graphed in the following manner: the enzyme concentrations were plotted against time in one-minute intervals over the course of 10 minutes. The rate of reactions (velocities) and enzyme activities were calculated in order to be used to analyze the reactivity of the enzyme and substrates. For Part B, students made five dilution solutions having the following concentrations respectively: 0.0025mM, 0.005mM, 0.01mM, 0.025mM, 0.05mM and then they were inserted into the spectrophotometer, which was first blanked using a “blank” sample containing sodium bicarbonate buffer, to obtain the absorbance values. The data were then graphed (Concentration (mM) on the x-axis and absorbance on the y-axis) to obtain a standard