Aim: To investigate the effect of Trypsin using a photographic film
Prediction: In this experiment there are two variables. Firstly, the pH. Changes in pH would alter or totally inhibit the enzyme from catalysing a reaction This change in the pH will affect the polar and non-polar intramolecular attractive and repulsive forces and alter the shape of the enzyme and the active site as well to the point where the substrate molecule could no longer fit, and the chemical change would be inhibited from taking place as efficiently or not at all. Every enzyme has an optimum pH range outside of which the enzyme is inhibited. Some enzymes like many of the hydrolytic enzymes in the stomach such as Pepsin and Chymotrypsin effective operate at a very low acidic pH. Other enzymes like alpha amylase found in the saliva of the mouth operate most effectively at near neutrality. I think that trypsin will work best at an alkali pH like 8 or 9. I think this because trypsin works in your duodenum and this has an alkali pH.
Secondly the temperature. Every enzyme has a temperature range of optimum activity. Modification of the lock and key hypothesis assumes that the active site has a certain amount of elasticity whereby the active site can expand or contract in a limited way in order to accommodate the substrate molecule. The analogy is like a hand fitting into a glove. The glove adjusts in shape and size to fit various sized hands within a certain range. This tolerance would explain why bogus molecules of slightly different size compared to the true substrate molecule could still be accommodated by the elastic active site. Small changes in temperature would distort the active site conformation but not so much that the active site could not still accommodate the substrate molecular size. PH changes which would also change the active site conformation but not so much that the active site could not flexibly accommodate the substrate molecule. The Induced Fit Model seems to explain why there is some flexibility in the edibility of the active site to accommodate other molecules and at limited temperature and pH ranges.
Prediction: In this experiment there are two variables. Firstly, the pH. Changes in pH would alter or totally inhibit the enzyme from catalysing a reaction This change in the pH will affect the polar and non-polar intramolecular attractive and repulsive forces and alter the shape of the enzyme and the active site as well to the point where the substrate molecule could no longer fit, and the chemical change would be inhibited from taking place as efficiently or not at all. Every enzyme has an optimum pH range outside of which the enzyme is inhibited. Some enzymes like many of the hydrolytic enzymes in the stomach such as Pepsin and Chymotrypsin effective operate at a very low acidic pH. Other enzymes like alpha amylase found in the saliva of the mouth operate most effectively at near neutrality. I think that trypsin will work best at an alkali pH like 8 or 9. I think this because trypsin works in your duodenum and this has an alkali pH.
Secondly the temperature. Every enzyme has a temperature range of optimum activity. Modification of the lock and key hypothesis assumes that the active site has a certain amount of elasticity whereby the active site can expand or contract in a limited way in order to accommodate the substrate molecule. The analogy is like a hand fitting into a glove. The glove adjusts in shape and size to fit various sized hands within a certain range. This tolerance would explain why bogus molecules of slightly different size compared to the true substrate molecule could still be accommodated by the elastic active site. Small changes in temperature would distort the active site conformation but not so much that the active site could not still accommodate the substrate molecular size. PH changes which would also change the active site conformation but not so much that the active site could not flexibly accommodate the substrate molecule. The Induced Fit Model seems to explain why there is some flexibility in the edibility of the active site to accommodate other molecules and at limited temperature and pH ranges.
