This enzyme kinetics experiment is designed to determine the optimum pH and temperature of the á-amylase enzyme. Using starch as a substrate, I was able to measure with a spectrophotometer the absorbance of light and determine how much of the substrate the enzyme had been transformed. Then by using calculations based on analysis, I proceeded to find that the optimum temperature for the enzyme to work is at 55°C and the optimal pH is 5. These were close to the results I hypothesized but not exactly because error was significantly there. These results are meant to benefit not only the commercial world but also the farmers that grow the barley from which á-amylase is harvested.
             Enzyme kinetics experiments try to determine the optimal situation for an enzyme to perform at its maximum efficiency (Vilet, 1996). Enzymes are a catalytic protein that lowers the activation energy of a reaction (Campbell, 2002). When an enzyme is in the presence of a substrate (the substance the enzyme is designed to change) it changes it and it itself does not change (Campbell, 2002). In the beginning, when the substrate is with the enzyme at its maximum concentration, the enzyme will change the substrate at its maximum rate and the time that the enzyme takes to meet a new substrate particle after finishing with another is negligible (Campbell, 2002). This is called the Vmax and the substrate concentration at which half of Vmax occurs is called KM (Vilet, 1996). Eventually as the enzyme changes more and more of the substrate the reaction rate will decrease and the enzyme will take longer to meet up with a substrate partner (Campbell, 2002). Now, enzymes work better in certain conditions and in other conditions they cannot work at all (Campbell, 2002). In this experiment I tried to determine the optimal conditions for the enzyme á-amylase. The enzyme á-amylase is collected from germinating barley seeds and is used for malt beve...