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4 uses of enzymes in an industry
4 uses of enzymes in an industry
4 uses of enzymes in an industry
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Research question:
What effects do different pH levels have on the rate of reaction of the enzyme?
Background information:
Catalysis is the increase in the rates of chemical reactions due to the participation of catalysts. Catalysts are substances that cause catalysis. An example of this is enzymes. Enzymes are proteins that speed up the rate of a chemical reaction of substrates. The substrates will be broken down or turn into products with the aid of enzymes. Enzymes and substrates are often said to fit like a “lock and key model” because each enzyme has exactly one matching type of substrates. This is due to the shapes of the substrates and enzymes’ activation sites. Only a specific substrate will bind to a specific enzyme due to the shape of the activation site. A different substrate will not fit in an enzyme, just like the wrong key will not fit into a lock. However, enzymes are not able to perform to their best at any given circumstance. As the activity of the enzyme is affected by its environmental conditions, changing the conditions can alter the rate of reaction by the enzyme. Naturally, the maximum rate of reaction would be produced at the enzyme’s optimum environmental conditions. For example, pepsin functions best in a strongly acidic environment because the acidic environment is the preferred condition of pepsin, allowing it to operate at its best. There are three different factors that affect the rate of chemical reactions: temperature, level of pH, and the enzyme and substrate concentration. At its optimum temperature, the enzyme will function at its best. This is the same for the other two factors. This lab will focus on one of them – the level of pH. More specifically, the relationship between the pH at which the ...
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...8. (Indicates the level of pH tested).
5. Pick one number from above.
6. Get 3 test tubes to test for one pH level (the one chosen from step 3).
7. Use a graduated cylinder to measure out 3 ml of H2O2.
8. Pour into one of the test tubes.
9. Measure and pour 3 ml of H2O2 into the remaining 2 test tubes.
10. Prepare10ml of the pH desired (should be the same as step 3).
11. Use a clean graduated cylinder to measure 3ml of step 10.
12. Pour into the test tube of step 8.
13. Use the pipette to drop about 2-3 drops of the enzyme into the same test tube.
14. Repeat step 13 with the remaining two test tubes of the same pH.
15. Wait 3 minutes for the reaction to occur.
16. Observe and measure, using a ruler, the height of O2 gas produced from the reaction.
17. Repeat steps 5-15, but with a different number for step 5.
18. Repeat step 17, with the last number (level of pH).
We used the pipette filler and filled the glucose rinsed pipette to add 10ml of 10% of glucose in test tube 0.
For example, substrate concentration, enzyme concentration, and temperature could all be factors that affected the chemical reactions in our experiment. The concentration of substrate, in this case, would not have an affect on how the bovine liver catalase and the yeast would react. The reason why is because in both instances, the substrate (hydrogen peroxide) concentration was 1.5%. Therefore, the hydrogen peroxide would saturate the enzyme and produce the maximum rate of the chemical reaction. The other factor that could affect the rate of reaction is enzyme concentration. Evidently, higher concentrations of catalase in the bovine liver produced faster reactions, and the opposite occurs for lower concentrations of catalase. More enzymes in the catalase solution would collide with the hydrogen peroxide substrate. However, the yeast would react slower than the 400 U/mL solution, but faster than the 40 U/mL. Based on this evidence, I would conclude that the yeast has a higher enzyme concentration than 40 U/mL, but lower than 400
The purpose of the experiment is to study the rate of reaction through varying of concentrations of a catalyst or temperatures with a constant pH, and through the data obtained the rate law, constants, and activation energies can be experimentally determined. The rate law determines how the speed of a reaction occurs thus allowing the study of the overall mechanism formation in reactions. In the general form of the rate law it is A + B C or r=k[A]x[B]y. The rate of reaction can be affected by the concentration such as A and B in the previous equation, order of reactions, and the rate constant with each species in an overall chemical reaction. As a result, the rate law must be determined experimentally. In general, in a multi-step reac...
6. Place the test tube in the beaker. Secure the test tube and thermometer to the retort stand using clamps. Begin heating the water bath gently.
Pipette 5cm cubed of casein suspension into one boiling tube and 5cm cubed of protease solution into another tube.
“Peroxidase is a heme-containing enzymes found in peroxisome (eukaryotic organelle) and can be obtained from a variety of plant tissues” (Coleman, 2015). Peroxidase breaks down different compounds and adds hydrogen to make it harmless. Peroxidase was a number of substrates such as cytochrome C and many more dyes (Ahmad, 2014). PH is 7 which is neutral and what is does to higher or lower the activity results in activity loss of an enzyme. The purpose of this lab is to observer effects different environments have on an enzymes (Lockwood, 2012). If the pH is changed then the speed of the enzymes will change (Urry, 2013). Prediction when the pH is changed of course it will speed up the enzymes because the pH changes the enzymes shape and when changing the enzymes shape is affects the function of the chemical
Enzymes have the ability to act on a small group of chemically similar substances. Enzymes are very specific, in the sense that each enzyme is limited to interact with only one set of reactants; the reactants are referred to as substrates. Substrates of an enzyme are the chemicals altered by enzyme-catalysed reactions. The extreme specific nature of enzymes are because of the complicated three-dimensional shape, which is due to the particular way the amino acid chain of proteins folds.
For this experiment, you will add the measured amount of the first sample to the measured amount of the second sample into its respectively labeled test tube then observe if a reaction occurs. In your Data Table, record the samples added to each test tube, describe the reaction observed, if any, and whether or not a chemical reaction took place.
3.) Divide your 30g of white substance into the 4 test tubes evenly. You should put 7.5g into each test tube along with the water.
From looking at the results I can conclude that when the pH was 3 and
The second test was to put 5 drops of the distillate into a test tube
Jim Clark. (2007). The effect of changing conditions in enzyme catalysis. Retrieved on March 6, 2001, from http://www.chemguide.co.uk/organicprops/aminoacids/enzymes2.html
2. In the large beaker, put water and boil it completely. After that, remove the beaker from heat. 3. Sample tubes (A-D) should be labeled and capped tightly.
The 6ml ½ strength stock solution was used for this experiment for dilution. That created the serial dilutions of (undiluted) full strength, ½ strength, ¼ strength, and 1/8 strength. 1 ml of the enzyme was added to each of the 4 spec tubes when ready to start recording enzyme concentration. Readings were recorded every 60 seconds for 5 minutes. After having the readings, the reaction rate was determined by using the following formula: (final absorbance- initial absorbance)/ time. From the first three minutes was how reaction rate was determined. Lastly, a graph was made to distinguish the change in reaction rate versus the concentration of the enzyme. Part 3 required similar steps as part 2, however, in the start of the dilution was a 0.024M catechol solution. This serial dilution required 5 tubes because the dilutions are to result in five different concentrations up to 1/16 strength of the catechol. Once the strengths in the regular tubes were added respectively to their spec tubes, immediate recordings of absorbance was done to each of the 5 spec tubes every 60 seconds for 5
tube. Add 6 mL of 0.1M HCl to the first test tube, then 0.1M KMnO4 and