It is hypothesized that the optimum pH of trypsin is 8. Three different pH levels were tested, and each level consisted of three trials. The pH of 5 showed an average absorbance of 0.021±0.002, the pH of 8 showed an average absorbance of 0.167±0.030, and the pH of 11 showed an average absorbance of 0.088±0.001. Based on the standard deviation, there was a lack of variability between each trial for the pH levels of 5 and 11, yet the trials of the pH of 8 varied greatly compared to the other levels. The p-value between pH 5 and 8 was 0.0011 and the p-value between pH 8 and pH 11 was 0.0106. Because p<0.05, each pH level was statistically significant from one another; hence the differences between the average absorbance values were due to the pH levels (experimental variable). The data collected in the experiment supports only our hypothesis, but not the proposition as a whole. The limitation of using only three pH levels is not enough data to conclusively state that the optimum pH of trypsin is truly 8.
Data was collected from groups who acquired …show more content…
The pH level of 8 showed an average absorbance of 0.167±0.030. The sources of variability consist of instrumental and operator errors. Instrumental errors include an inconsistent spectrophotometer and poorly calibrated micropipettes. Operator errors include unknowingly allowing trypsin to decay in an environment of room temperature, as well as the short length of incubation when mixing the trypsin, azocasein, and the reaction buffer. The potential sources that proved the most problematic include the condition of trypsin and the length of incubation. Trypsin must be kept in a cold environment when not in use, and the incubation of the samples must be long enough for the proteolysis to take place in the constant condition of 37°C for each trial. It is clear that in each trial for the pH 8, the extent of the breakdown of azeocasein
Data was collected from groups who acquired …show more content…
The pH level of 8 showed an average absorbance of 0.167±0.030. The sources of variability consist of instrumental and operator errors. Instrumental errors include an inconsistent spectrophotometer and poorly calibrated micropipettes. Operator errors include unknowingly allowing trypsin to decay in an environment of room temperature, as well as the short length of incubation when mixing the trypsin, azocasein, and the reaction buffer. The potential sources that proved the most problematic include the condition of trypsin and the length of incubation. Trypsin must be kept in a cold environment when not in use, and the incubation of the samples must be long enough for the proteolysis to take place in the constant condition of 37°C for each trial. It is clear that in each trial for the pH 8, the extent of the breakdown of azeocasein