Bacillus Linchenilormis Experiment
Throughout this work, a correlation between the enzyme activity and temperature existed. The data for both showed that at the temperature extremities the lower the enzyme activity was; except for the bacterial enzyme at 0°C. At high temperatures, an enzyme denatures or changes shape, making it difficult or impossible for a substrate to bind, and at low temperatures, the frequency and rate of reaction decreases causing for a halt in product formation (Pitzer et.al., 2012). Thus, showing that enzymes need to be in their optimal environments to work properly. Bacillus lincheniformis and Aspergillus oryzae are both organisms that live that in medium temperature environments. Bacillus Linchenilormis has an optimal temperature of 45°C to 50°C, whereas …show more content…
Both enzymes denatured at 85°C base on the black/blue liquid color in the spot plate, meaning that the temperature was above the temperature needed to function properly. At 0°C, the bacterial enzyme had the highest enzymatic activity, disproving the hypothesis. However, the fungal amylase had low enzymatic activity, it had the second darkest liquid color in the spot plate. At 25°C, both enzymes had the third darkest color, showing some starch breakage and enzyme activity. At 55°C, the bacterial amylase had the second highest enzyme activity, with the exception of the 0 minute mark, which just contains starch mix with iodine. The fungal amylase showed the highest enzyme activity was at this temperature, with the lightest color from all the temperatures. Thus the individual group data, showed bacterial amylase to have an optimal temperature at 0°C, and fungal amylase showed to have an optimal temperature at 55°C. Nevertheless, the class data does not support these findings by the individual group. Base on the class data, both bacterial amylase and fungal amylase have an optimal temperature of 55°C, proving the hypothesis. This difference between the class data and the individual data shows that errors must have occurred while preforming the bacterial enzyme
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