The optimum temperature probably reflects the soil temperatures in areas where turnips normally grow. Why such an extreme result? We cooked our enzyme. When you boil an egg, it goes from liquid to solid because the heat breaks and reconfigures the hydrogen bonds between amino-acids in the egg proteins. You permanently change the shape of the proteins, and so permanently change their qualities in this case, texture. The same thing happened to our enzyme.
The heat-induced reconfiguration of the hydrogen bonds permanently changed the shape of our enzyme, which caused it to cease functioning.
When the shape of a protein is permanently changed, we say it has been denatured. Graphing Reaction Rates. Aside from curves showing enzyme optima, there is another way to compare reaction rates under varying treatments.
When we graphed our initial reactions on the spectrophotometer, we saw absorbance on the y versus time on the x. Thus, slope or m equaled the reaction rate, and the greater the slope, the faster the reaction rate. A slope of zero would be no reaction. For example, people who tried to take reaction readings from their blank tubes saw a flat line. We recorded the slope of each line and then compared these between all our tests by graphing them as rate on the y versus environmental variable for example, temperature.
Another way to compare the reaction rates under different conditions like different temperatures or pHs would be to place the best fit lines of each different absorbance vs. The steepest line would be the fastest reaction and thus the optimum condition for the enzyme for example, room temperature. Concentration Effects.
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The enzyme has an affinity towards hydrogen peroxide as its substrate in the presence of orthodianisidine as a chromogenic substrate. Enzyme activity was enhanced with calcium and magnesium, whereas sodium, potassium, and manganese inhibit the enzyme activity.
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