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Enzyme Kinetics

             This experiment was performed to determine the factors that influence enzyme reaction rates. Amylase enzyme activity was measured through its absorption rate in spectrophotometer, using light with a wavelength of 560 nm. We compared the absorbance rates by varying temperatures in one experiment and increasing levels of pH in another. The highest levels of absorbance were found in samples with a temperature of 55 deg C and in pH levels measuring 5.5. It was found that amylase and starch reaction rates were highest when the temperature and pH had the highest level of absorbance. .
             "In living organisms, biochemical reactions are facilitated by catalyst, substances that accelerate reactions but are not consumed or permanently changed in the process (Vilet, 1993)." An enzyme is very specific in the reactions in which it undergoes: it contains an active site that allows only certain reactants to bind to it. In the experiment of enzyme kinetics, we examined the absorbance levels and rate of reactions of amylase and starch with varied temperature and pH levels. We hypothesized that environmental factors, temperature and pH level, increase reaction rates and thus we expected reaction rates to have a greater net conversion of substrates than those with a lower temperature and pH levels.
             Now in order to maintain its specific function, an enzyme must retain the specialized shape of its active site. "Environmental factors such as temperature and pH levels have been known to alter the conformation of a protein (Neilands, 1955)." The goal of this is experiment is to find the optimum levels of temperature and pH that maximize the reaction rate between enzyme amylase and substrate starch without causing "instability or denaturation (Neilands, 1955)." .
             Material and Methods.
             To calibrate the spectrophotometer at zero absorbance, a blank control tube prepared with 5 ml of distilled water and 0.

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