The premise of this lab is to measure our enzymatic activity of Alkaline phosphatase, we began measuring our activity by applying different substrate concentration of p-nitrophenyl phosphate in relationship to absorbance over the span of 70 seconds, the data obtained in table 5.1, the different substrate concentration 0.9mM, 0.675mM, 0.45mM, 0.225mM, 0.09mM, 0.045mM, 0.0225mM. keeping our enzyme constant at 100μL, what we concluded is a significant decrease on the absorbance as we decrease the substrate concentration, for example our initial reading of absorbance at 0.09mM concentration was 0.558, the same reading at 0.0225mM was significantly lower (0.176) thus indicating that substrate concentration does influence absorbance if the enzyme concentration remains constant. …show more content…
This time, we reduced the enzyme by half thus using only 50μL of our enzyme, our obtained result indicated just as we predicted, that the absorbance value regardless of the different substrate concentration used would approximately equal to half of the absorbance obtained in table 5.1. for example when comparing the absorbance 0.05mM in table 5.1 at the first 10 second (0.178) to 0.05mM in table 5.2 i.e half enzyme we obtained (0.111) which was almost half of 0.05mM absorbance with 0.044 difference. Thus concluding that when using half of the enzyme amount, the absorbance will be reduced to half as much as that of using an enzyme in full