Enzyme Kinetics of Beta-Galactosidase

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Abstract This experiment is to study and measure the enzyme activity of β-galactosidase in the different concentrations of o-Nitrophenylgalactoside (ONPG) using a spectrophotometer. The spectrophotometer was also set at 420nm, a wavelength which is best for recording the absorbance values for the experiment. From the results, 0.9mM ONPG solution has the highest absorbance and 0.1mM ONPG solution has the least. Also, 0.5mM ONPG solution has the highest rate of enzyme activity and it is the most efficient as the enzyme activity of the ONPG solution continues even though the other concentrations of ONPG solution has already stopped the enzymatic reactions as the substrate is already used up. Introduction This experiment is to study and…show more content…
This indicates that the lowest concentration of the ONPG solution has the lowest o-Nitrophenol (ONP) and galactose concentration in the solution, thus having the lowest absorbance. However, the highest concentration of the ONPG solution does not show that it has the highest ONP and galactose concentration. 0.9mM ONPG solution, however, has the highest ONP and galactose concentration as compared to the 1.0mM ONPG solution. The gradient of the graph shows the rate of enzyme activity. The steeper the gradient, the higher the rate of enzyme activity. 0.5mM ONPG solution has the highest rate of enzyme activity for the first 20 seconds, as shown by the steepness of the graph. Most of the enzymatic reactions for the different concentrations of ONPG solutions also stopped before 200 seconds, except for 0.5mM ONPG solution which continued to increase until 320 seconds. Conclusion From the results, we can conclude that 0.9mM ONPG solution has the highest absorbance value and 0.1mM ONPG solution has the least absorbance. However, 1.0mM ONPG solution, which has the highest concentration, does not have the highest

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