Alkaline Phosphatase Enzyme Lab Report

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In part one, the effects of pH on the alkaline phosphatase enzyme (ALP) were observed. The reaction in tube 2 caused the absorption to move closer to zero, but the absorption did not change much in the ten minute time period as seen in table 2 and figure 1. The reaction in tube 2 was the only reaction that the numbers decreased rather than of increased. Tube 2’s rate of reaction is negative as can be seen in figure 2.
In tube 3, the absorption increased as the reaction progressed, and the absorption was the highest in tube 3 compared to the other tubes. Tube 3 had the highest rate of reaction of the three tubes as seen in figure 2. The reaction occurred much faster in tube 3 than it did in tube 2. Tube 3’s pH had the greatest
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The effect of the temperature is similar to the effect of the concentration; as the temperature increased the rate of reaction also increased as seen in figure 6. In the solution with the highest temperature, the reaction occurred the quickest. In the 20°C and the 32°C solutions, the temperature had similar effects of the rate of the reactions as seen in table 5 and figure 5, but the reaction in the 32°C solution was slightly faster. Figure 5 Figure 6

Discussion In part one of the experiment, the effects of pH on the ALP enzyme were determined. The optimal pH for this enzyme was greater than two, but it was less than 10. The optimal pH was close to neutral because the rate of the reaction was quickest when the pH was seven. The solution with the pH of two had a negative rate of reaction, which means that the acidic pH did not allow the reaction to occur. In the solution with a pH of ten, the reaction was slower than the solution with a pH of seven, but it was much faster than the solution with a pH of two. The reaction still occurred at an increased rate with a pH of

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