List The Substrate And The Subunit Product Of Amylase.

Question: list the substrate and the subunit product of amylase

Answer: The substrate of amylase is starch and carbohydrate. The subunit product of amylase is maltose and glucose.

Question: what effect did boiling have on enzyme activity and why

Answer: The boiling denatured the enzyme and inactivated it. It's no longer able to function because chemical bonds holding its structure together break down, it looses its 3/d structure and can't bind to target substrate molecule

Question: at what pH was the amylase activity the most active. Describe the significance of this result

Answer: Amylase was most active at pH 7.0. This is significant because this is around the same pH as the mouth.

Question: describe the need for controls and give an example used in this activity

Answer: Controls are necessary to validate the results of the experiment (specifically negative results with negative controls) and provide a known standard against which comparisons can be made. Negative controls are used to determine whether there are any contaminating substances in the reagents. Tube #5 is an example where the enzyme that tests for contaminating glucose in the starch or the buffer is absent.

Question: describe the significant of using a 37 degree c incubation temp to test salivary amylase activity

Answer: it is around the same temperature as body temperature so it should be ideal for the enzyme.

Question: Describe why the results in tube 1 (amylase, startch and ph 7) and tube 2 (amylase glucose ph 7) are the same

Answer: because in tube 1, the amylase is hydrolyzing the starch to glucose and in tube 2, the glucose is already present in the hydrolyzed form

Question: describe the results in tube 3 (amylase, cellulose and ph 7)

Answer: show that salivary amylase does not digest cellulose as demonstrated by the negative results from theBenedict's test.

Question: describe the usual substrate for peptidase

Answer: peptides and proteins.

Question: explain how bacteria can aid in digestion

Answer: breaking down cellulose which we do not digest as we dont produce cellulase. Helps break down things we can't

Question: describe the effect that boiling had on pepsin and how could you tell that it had that effect

Answer: Boiling inactivated the pepsin. This is evidenced by the fact that no activity was seen with Tube #1. However, the enzyme was very active in Tube #2.

Question: was your prediction correct about the optimal pH for pepsin activity? Discuss the physiological correlation behind your results

Answer: The correct prediction is pH 2.0. This is because pepsin is most active at the pH of gastric juice which is about pH 2.0.

Question: what do you think would happen if you reduce the incubation time to 30 min for tube 5 (pepsin, BAPNA, ph 7)

Answer: it is possible that no digestion of protein would be seen since only a small amount is seen.

Question: Why can't you fully test the lipase activity in tube 5? (lipase, veg oil, bile salts, ph 2)

Answer: Measurement of lipase activity uses a decrease in pH. Since the pH in Tube #5 is already very low, it is difficult to tell if fatty acids are released.

Question: which tube has the highest lipase activity. discuss possible reasons why it may or may hve not matched

Answer: Tube #1, pH 7.0, which approximates the pH of the small intestine.

Question: explain why pancreatic lipase would be active in both the mouth and the pancreas

Answer: Since the activity of pancreatic lipase is highest at pH 7.0, the enzyme should be active in the mouth and the pancreas where there is a similar pH

Question: describe the process of bile emulsification of lipids and how it improves lipase activity

Answer: Bile serves to mechanically break up large globules of fat and produce small droplets that effetely increases the surface area of the lipids.