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Trypsin Lab Report

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Abstract
The pH of our duodenum fluctuates from acidic (pH 2) to alkaline (pH 7.5), (Woodtli & Werner, 1995). Enzymes such as Trypsin, work in our duodenum to speed up the chemical reactions which break down macromolecules and extract nutrients and energy from the food we eat. Since enzymes change activity depending on pH due to changes in their tertiary structure, we wanted to assess the effects of pH on the Trypsin enzymatic activity. To address our question, we conducted the reaction in which the substrate BAPA and TRIS buffer were mixed with Trypsin extract, and the rate of reaction was measured as product appearance (p-nitroanaline) over time using a spectrophotometer. We conducted 6 replicates for the reactions at pH 4, pH5, pH6, pH7, …show more content…

From our data, the optimal pH range for Trypsin was found to be pH 7-10 (over the range of pHs 4-10). We found that the average reaction rate of the Trypsin catalyzed reaction increased significantly each time as we increased the pH from 4 to 5, from 5 to 6, from 6 to 7, from 6 to 8, from 6 to 9 and from 6 to 10, however there is no significant difference between the reaction rates at pHs 7, 8, 9 and 10. We found that at pHs lower than the experimentally determined optimal pH range of Trypsin (7-10), there was a decrease in enzymatic activity compared to the activity at pH 7-10, but at pHs higher than this optimal pH range (up to a pH of 10), there was no significant effect of the pH on the enzymatic activity. Thus according to the results of our experiment, fluctuations in pH (within the range of pH 4-10) in the duodenum would only significantly decrease the trypsin enzymatic activity below optimal, when the pH fluctuates and decreases below a …show more content…

Basic secretions from the pancreas then enter the small intestine to neutralize the pH-decreasing effect of the acidic chyme. Thus these basic and acidic fluid secretions in the duodenum, cause the pH in the duodenum to fluctuate from an acidic pH of 2 to a basic pH of 7.5 (Woodtli & Werner, 1995). We wanted to investigate the question of how these fluctuations of pH in the duodenum affect the activity of the enzyme Trypsin. Enzymes play a very important physiological role in the human body because they speed up the rates of reactions vital to our survival. Enzymes bind to specific substrates and configure their positions, geometry or interactions relative to one another in such a way, that the activation energy required for a reaction to occur is lowered, and thus the reaction rate is increased. The activity of an enzyme depends on many environmental factors such as pH and temperature, because changes in temperature and pH affect the intermolecular interactions between amino acids in the backbone, holding the tertiary structure of the enzyme together. Thus each enzyme has an optimal pH range, below which, and above which its activity declines. Trypsin is an important enzyme that catalyzes the breakdown of specific peptide bonds in the duodenum of the small intestine so that we can extract nutrients and energy from the proteins we eat (Nelson & Cox, 2013). Trypsin is a

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