How Does Temperature Affect The Rate Of An Enzyme Catalysed Reaction

The effect on rate of an enzyme catalysed reaction by different objectives which include effect of substrate, temperature, ph and effect of a competitive inhibitor phosphate ions. This is determined by the reaction of hydrolysis by p-nitrophenylphosphate (PNP) as a substrate by the enzyme phosphatase.
Abstract
The hydrolysis of p-nitrophenyl phosphate has been studied in human red blood cells. To see if hydrolysis was related to the functioning of the sodium pump. Acid phosphatase catalysis’s the hydrolysis of p-nitophenyl phosphate under four different objectives ph, temperature, substrate inhibition and a competitive inhibitor. The phosphatase and PNP were placed in test tubes with different concentration of each but under different objectives. The concentration of the enzyme and substrate were the same for each experiment. It was shown that the Vmax was 0.286 and the Km was 0.0114. As the valve of Km is small this shows that there is a high enzyme substrate affinity. There were some anomalous results obtained within experiment 2 and experiment 3 these may be due to experimental or human errors.

Introduction
This may have occurred due to an experiment error such as measuring error. Using a smaller pipette would have given a more accurate measurement also an air bubble may have occurred whilst using the pipette altering the measurements in each test tube.
Within the last experiment it was looking at the effect of an inhibitor phosphate ion on the rate of reaction between the enzyme phosphatase and substrate PNP. As the concentration of phosphate ions increases a higher concentration if PNP is needed to attain the reaction velocity. Looking at graph 6 there is an interception on the y-axis which indicates phosphate ions are competitive inhibitors. Even though the slope increases the intercept is unchanged because a competitive inhibitor does not alter the Vmax but increases Km.
Question