Comparing Free to Immobilised Amylase Enzyme in Its Catalysis Rate Method: First of all, the Immobilised enzymes need to be made. The method used to create these immobilised enzymes would be Micro encapsulation. This means that the enzyme used, in this experiment being Amylase, is encapsulated inside Sodium alginate. The enzyme was believed to act quickly, so the enzyme would have to be slightly diluted in order to get a good range of results. !0cm³ of Amylase will be added to 20cm³ of Sodium alginate, and then mixed. Using a pipette, the Sodium Alginate - Amylase mix is dropped into Calcium Chloride, and this will form the beads of Immobilised enzymes needed for the experiment. As soon as Sodium Alginate touches Calcium Chloride, it solidifies and this traps the enzyme inside. The good thing is that the beads are semi permeable, so the substrate can penetrate the bead and get to the enzyme. As I'm sure you are well aware, enzymes do not get used up in a catalysis reaction, so the beads can be used again and again to our benefits. The Immobilised enzymes will be kept in water to prevent cracking and drying out and about 110 beads will be made. The free enzyme will not take so long to prepare. The enzyme itself, Amylase had a concentration percentage of 0.125%, which is quite strong, to my knowledge. Judging from previous experiments, this has been known to work quickly, so small time intervals will be used in order to get a wide range of results. In order to keep this experiment a fair test, the free enzyme must be diluted to the same extent as the Immobilised enzyme, so 10cm³ of enzyme was added to 20cm³ of distilled water. M... ... middle of paper ... ... of enzyme in the 2cm³ as they may have been 36 beads instead of 37. Its possible that it could have got infected with bacteria, and this would have bred in the test tube, seeing as it was just over optimum. The bacteria could have got in the way of the enzyme and substrate and caused the reaction to take longer then necessary. Again I say that it is a possibility. Human error may also have caused the anomaly. Maybe too much starch was added to the test tube, or too much Buffer solution. The only way to get rid of this is to repeat the experiment 3 times and then take an average. This would have been done if given more time. Overall, the free enzyme works quicker than the immobilised enzyme at optimum conditions and the immobilised enzyme works better than the free at higher temperatures, exceeding optimum.
The alternate hypothesis is that there exists an optimal pH level for catecholase enzyme in which the catecholase enzyme can operate with the highest possible
Kinetics of Ester Hydrolysis Catalyzed By Imidazole Experiment 3. Ban He Lab Partner: Colton Kincy TA: Ally Fairman September 19, 2014. Abstract: The purpose of the experiment was to study the kinetics of the hydrolysis of ester, p-nitrophenyl acetate (NPA) that is catalyzed by the buffer imidazole (Im).
The purpose of this experiment was to discover the specificity of the enzyme lactase to a spec...
== Amylase is an enzyme found in our bodies, which digest starch into
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.
Investigating the Effect of Substrate Concentration on Catalase Reaction. Planning -Aim : The aim of the experiment is to examine how the concentration of the substrate (Hydrogen Peroxide, H2O2) affects the rate of reaction. the enzyme (catalase).
I have chosen to vary the concentration of the enzyme catalase, as it is simple to do in the laboratory, and will obtain easy to interpret results. Therefore, all the other variables will be kept constant to make sure the experiment is fair. Keeping the experiment fair: All of the variables with the exception of the concentration of catalase will remain the same, to make sure that the results obtained are not influenced by anything other than the concentration.
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.
The three-dimensional contour limits the number of substrates that can possibly react to only those substrates that can specifically fit the enzyme surface. Enzymes have an active site, which is the specific indent caused by the amino acid on the surface that fold inwards. The active site only allows a substrate of the exact unique shape to fit; this is where the substance combines to form an enzyme- substrate complex. Forming an enzyme-substrate complex makes it possible for substrate molecules to combine to form a product. In this experiment, the product is maltose.
From looking at the results I can conclude that when the pH was 3 and 5. No oxygen was produced, therefore no reactions were taking place. This was because the pH had a high hydrogen ion content, which caused the breaking of the ionic bonds that hold the tertiary structure of the enzyme in place of the syringe. The enzyme lost its functional shape.
If I was to do this experiment again I might use a Fungi amylase to
Abstract: Enzymes are catalysts therefore we can state that they work to start a reaction or speed it up. The chemical transformed due to the enzyme (catalase) is known as the substrate. In this lab the chemical used was hydrogen peroxide because it can be broken down by catalase. The substrate in this lab would be hydrogen peroxide and the enzymes used will be catalase which is found in both potatoes and liver. This substrate will fill the active sites on the enzyme and the reaction will vary based on the concentration of both and the different factors in the experiment. Students placed either liver or potatoes in test tubes with the substrate and observed them at different temperatures as well as with different concentrations of the substrate. Upon reviewing observations, it can be concluded that liver contains the greater amount of catalase as its rates of reaction were greater than that of the potato.
Purpose: This lab gives the idea about the enzyme. We will do two different experiments. Enzyme is a protein that made of strings of amino acids and it is helping to produce chemical reactions in the quickest way. In the first experiment, we are testing water, sucrose solution, salt solution, and hydrogen peroxide to see which can increase the bubbles. So we can understand that enzyme producing chemical reactions in the speed. In the second experiment, we are using temperature of room, boiling water, refrigerator, and freezer to see what will effect the enzyme.
In this experiment, researchers used different measurements of catechol and 1cm of potato extract. Researchers hypothesized that the increase in substrate would level out the enzyme activity by
35, 40, 45, 50, 55, 60, 65, 70, 75 and 80 beads. The experiment was