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Hypothesis of examing the effects of optimal pH on enzyme salivary amylase
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Questions & Tables from Experiment Three
1. What is the optimal pH for salivary amylase activity and how does it compare with the pH at which the enzyme is normally found?
• The optimum pH level for salivary amylase is approximately 6.8. Any change of pH below or above the optimum pH decreases the rate of enzyme action. The changes in pH can lead to changes in the ionization state of the substrate or the enzyme or both. The optimal pH level is slightly acidic whereas the enzyme is a little more basic.
2. The pH inside most animal’s stomachs is usually between 3 and 4. How much dietary starch is likely to be converted to maltose in the stomach relative to the mouth and esophagus?
• I believe that the level of dietary starch that is converted to maltose relative to the mouth and esophagus will vary from person to person. It will vary due to the fact that each individual will have a different pH levels within their body
3. What is the optimal temperature for salivary amylase activity and how does it compare with the temperature at which the enzyme normally acts?
• I believe that the optimal temperature for salivary amylase activity would be 37 degrees Celsius or 98.6 degrees Fahrenheit. The reason I believe this, is because the human body runs at a temperature of approximately 98.6 degrees
If there is too much of the salivary amylase in comparison to the starch solution, then it may break it down much faster than it should or it may overwhelm the solution and cause an inaccurate result. The same if there was not enough salivary solution in comparison to the starch solution. It may take longer to show any results if there is too much starch solution. Another thing to consider is the concentration of the starch solution. If the concentration of the solution is too concentrated, then it may not give accurate
After conducting this experiment and collecting the data I would have to say that the optimal temperature for enzyme activity would have to be room temperature which in my experiment was thirty-four degrees Celsius. I came to this answer because the glucose test strip showed that at room temperature there was more glucose concentration that at either of the other temperatures. Due to temperature extremes in the boiling water the enzymes could no longer function because the breakdown of lactose stopped. The cold water also hindered the breakdown of the lactose but as the water warmed the enzymes were more active which can be seen in the results for the cold water at 20 minutes B. Describe the relationship between pH and the enzymatic activity of lactase.
The affects of pH, temperature, and salt concentration on the enzyme lactase were all expected to have an effect on enzymatic activity, compared to an untreated 25oC control. The reactions incubated at 37oC were hypothesized to increase the enzymatic activity, because it is normal human body temperature. This hypothesis was supported by the results. The reaction incubated to 60oC was expected to decrease the enzymatic activity, because it is much higher than normal body temperature, however this hypothesis was not supported. When incubated to 0oC, the reaction rate was hypothesized to decrease, and according to the results the hypothesis was supported. Both in low and high pH, the reaction rate was hypothesized to decrease, which was also supported by the results. Lastly, the reaction rate was hypothesized to decrease in a higher salt concentration, which was also supported by the results.
b) Comprehensive diagnostic chemistry panel with significantly increased amylase (1626 with normal being 300-1100 U/L), total
Using a Bunsen burner, tripod and beaker of water 100 degrees could also be tested and 0 degrees was tested by using ice. (I didn’t investigate the 80 degrees temperature). Fair test: Below is a list of things that were kept the same throughout the investigation: Volumes of lipase and milk (by using syringes); volumes of phenolphthalein and sodium carbonate (using pipettes); (best volumes from the preliminary work were used). Each temperature was repeated three times to get a good average. The milk and lipase were equilibrated to the right temperatures before the lipase was added to the milk.
The independent variable for this experiment is the enzyme concentration, and the range chosen is from 1% to 5% with the measurements of 1, 2, 4, and 5%. The dependant variable to be measured is the absorbance of the absorbance of the solution within a colorimeter, Equipments: Iodine solution: used to test for present of starch - Amylase solution - 1% starch solution - 1 pipette - 3 syringes - 8 test tubes – Stop clock - Water bath at 37oc - Distilled water- colorimeter Method: = == ==
In this experiment as a whole, there were three individual experiments conducted, each with an individualized hypothesis. For the effect of temperature on enzyme activity, catalase activity will be decreased when catalase is exposed to temperatures greater than or less approximately 23 degrees Celsius. For the effect of enzyme concentration on enzyme activity, a concentration of greater or less than approximately 50% enzymes, the less active catalase will be. Lastly, the more the pH buffer deviates from a basic pH of 7, the less active catalase will be.
Carbohydrate digestion begins in the saliva and stomach where alpha-amylase hydrolyses alpha-1, 4 glycosidic bonds between glucose molecules in starch, forming maltotriose, the disaccharide maltose and dextrin’s made of five to ten glucose molecules (Lim, 2007). The disaccharides sucrose and lactose come directly from food. There are four enzymes found on the brush-border membrane responsible for hydrolysing sucrose, lactose and the products of starch break down, into monosaccharaides so that they can be absorbed (Lieberman et al, 2007). These enzymes are known as glycosidases and include; glucoamylase, lactase, trehalase and sucrase isomaltase (Lieberman et al, 2007). Sucrase isomaltase...
Investigating the Rate of Reaction between Amylase and Starch. Plan Aim: To be able to The aim of this investigation is to find out whether the volume of amylase affects the rate of reaction between amylase and starch. Prediction: I predict that the greater the volume of amylase then the faster the rate of reaction between the starch and amylase. I predict this because of the lock and key hypothesis.
arg.gov.sk.ca - arg.gov.sk.ca - arg.gov.sk.ca - arg.gov.sk.ca - arg.gov Carbohydrates supply 80-90% of dietary energy. Sugars, starch, cellulose and related substances are carbohydrates. Starch is more easily digested than cellulose. Grains are easy to digest as they are 60-80% starch. A recent study conducted by Sharon R. Bullimore et al.
Investigating the Effect of Enzyme Concentration on the Hydrolysis of Starch with Amylase Aim: Investigate the effect of enzyme concentration on the rate of an enzyme-controlled reaction. Using amylase and starch as my example. Introduction: I am investigating the effect of the concentration of the enzyme, amylase on the time taken for the enzyme to fully breakdown the substrate, starch to a sugar solution. The varied variable will be the concentration and all other variables are going to be fixed. The different concentrations will be: 0.5% 0.75% 1.0% 1.5% 2% An enzyme is a class of protein, which acts as a biological catalyst to speed up the rate of reaction with its substrates.
When the solution remains the same, it means the solution is negative control and does not have sugar. The presence of starch can be detected by using the Lugol’s iodine solution. If the unknown A, B, C milk samples turn to a dark blue color during the Lugol’s test, then these samples are positive control and also contain starch in them. But if the solutions turn to yellowish brown, it means these solutions are negative control
Influence of Temperature on the Activity of Potato Catalase Hypothesis That the higher the temperature the higher the reaction rate of potato catalyse to a point were denaturing occurs in the enzyme and the reaction rate of the potato catalase drops off. Prediction The rate of Catalase activity will be faster at higher temperatures until a point, because at higher temperatures there are more chances of collisions between the enzyme's (Catalase) active site and the substrate (hydrogen peroxide). However the rate depends on the active site being able to join with the substrate, and at higher temperatures the enzyme can be denatured, which changes the shape of the active site which thus prevents the reaction from happening. At first, as the temperature increases the activity of the Potato catalase also increases this is because the collision rate of the enzyme with the hydrogen peroxide is increased.
If I was to do this experiment again I might use a Fungi amylase to
The Effect of pH on the Activity of Catalase Planning Experimental Work Secondary Resources Catalase is a type of enzyme found in different types of foods such as potatoes, apples and livers. It speeds up the disintegration of hydrogen peroxide into water because of the molecule of hydrogen peroxide (H2O2) but it remains unchanged at the end of the reaction.
According to the graph on amylase activity at various enzyme concentration (graph 1), the increase of enzyme dilution results in a slower decrease of amylose percentage. Looking at the graph, the amylose percentage decreases at a fast rate with the undiluted enzyme. However, the enzyme dilution with a concentration of 1:3 decreased at a slow rate over time. Additionally, the higher the enzyme dilution, the higher the amylose percentage. For example, in the graph it can be seen that the enzyme dilution with a 1:9 concentration increased over time. However, there is a drastic increase after four minutes, but this is most likely a result of the error that was encountered during the experiment. The undiluted enzyme and the enzyme dilution had a low amylose percentage because there was high enzyme activity. Also, there was an increase in amylose percentage with the enzyme dilution with a 1: 9 concentrations because there was low enzyme activity.