The optimum condition for the amylase enzyme is at pH = 6, temperature, T = 50⁰C and substrate concentration, = 1.5 %. The absorbance value is determine using the spectrophotometer. Then, the hydrolysis process is let to happen.
Amylase solution is mixed with starch solution after being let to sit in a certain temperature of water bath for a period of time. The method of determining the Michaelis Constant, Km used in the experiment is by Double Reciprocal Method. The main objective of the experiment is to investigate the enzyme activities and kinetics based on few parameters such that difference in pH, temperature and concentration of substrate. Therefore, pH 6 is the most optimum pH for the enzyme activity. Lastly, for the effect of pH, the graph showed that the enzyme activity increased from pH 5 until pH 6 and decreased until pH 7 and later increased again until pH 9. For the effect of temperature, the optimum temperature for the enzyme obtained from the graph is at 50℃, which the enzyme activity is at 2.421 x 10-7 mol/min. Based from the graph of effect of substrate concentration, it shows the bell shaped curve pattern rather than straight linearly line as in the standard curve graph and the ideal condition of the amylase enzyme is obtained at substrate concentration, = 1.5%, in which the enzyme shows the maximum rate of activity at this concentration. The double reciprocal method was used in order to find Michaelis constant, Km. The effects of temperature, pH and substrate concentration on the enzymatic activity were studied. Enzymes take part in the reaction where the catalyst provides an alternative reaction pathway.
Enzymes are biological catalysts, in which it is specific to only one type of reaction and to one small group of reactants called substrates.
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