ap bio Enzyme Catalysis

Topics: Catalysis, Enzyme, Catalase Pages: 5 (1007 words) Published: April 6, 2014

Enzyme Catalysis
Introduction: Enzymes are produced by living organisms as proteins. These enzymes perform as catalysts to bring about a chemical reaction. In fact, most reactions are catalyzed by enzymes during reactions in the cell or in the human body. A catalyst that enzymes pose ad are by definition substances that are capable of initiating or speeding up a chemical reaction. Catalyst are not a necessity during a chemical reaction, they are just used to speed up a chemical reaction. This event of speeding up a reaction with a catalyst is specifically known as catalysis and the speeding up of a chemical reaction through the use of an enzyme is known as enzyme catalysis. One result of an enzyme-catalyzed reaction is a reduction in the energy required to activate the reaction of the substrate molecule. This is s that the product (p) of the reaction is formed. In this type of reaction the substance that is acted upon is substrate (s). This reaction is shown through the formula: E+S → ES → E+P

This is the most basic form of the enzyme-catalyzed reaction formula. An enzyme that catalyzes the reduction of hydrogen peroxide is specifically known as catalase. This chemical reaction that is most catalyzed by catalase H2O2 decomposition to form water (H2O) and oxygen (O2). This chemical reaction is represented by the formula: 2 H2O2 → 2 H2O + O2 (gas)

Hypothesis: If the chemical reaction, H2O2 decomposition, is catalyzed by an enzyme, then the rate of the chemical reaction will increase.

Materials (part 2A): Part One
10 mL of 1.5% H2O2
50-mL glass beaker
1 mL catalase
2 10-ml pipettes and pipette pumps
Materials (part 2A): Part Two
5 mL of catalase
Boiling water bath
1 test tube
Test tube rack
10 mL of 1.5% H2O2
50 mL beaker
2 10-mL pipettes and pipette pumps
Materials (part 2A): Part Three
10 mL of 1.5% H2O2
50 mL beaker
Liver
Syringe
Materials (part 2D):
70 mL of 1.5% H2O2
70 mL of H2SO4
6 mL of catalase solution
13 plastic, labeled cups
1 10-mL syringe
1 5-mL syringe
1 60-mL syringe
a sheet of white paper
a timer
30 mL of KMnO4

Methods (part 2A): The first part in observing the reaction being studied is to transfer 10 mL of 1.5% H2O2 into a 50-mL glass beaker, then add 1 mL of the fresh catalase solution. During this step bubbles should begin to appear as a result the breakdown of H2O2 by catalase. The bubbles created are known as O2. Remember to keep the freshly made catalase solution on ice consistently. The second part of the part 2A is to demonstrate the effect of boiling an enzymatic activity. To do this transfer 5 mL of purified catalase extract to a test tube and place it in a boiling water bath for five minutes. After that 10 mL of 1.5% H2O2 into a 50-mL glass beaker and add 1 mL of the cooled, boiled catalase solution. Compare this reaction to the reaction using the unboiled catalase. The third part of part 2A is to demonstrate the presence of catalase in living tissue. To do this cut 1 cm3 of potato or liver, macerate it, and transfer it into a 50-mL glass beaker containing 10 mL of 1.5% H2O2. Methods (part 2D): To measure how much substrate is disappearing over time is necessary in determining the course of an enzymatic reaction.What will need to be measured is the amount of substrate that is decomposed after 10 seconds, 30 seconds, 60 seconds, 90 seconds, 120 seconds, 180, and 360 seconds, but remember to set up all of these at the same and do them at once to save precious lab time. For the 10 second experiment first put 10 mL of 1.5% H2O2 in a clean 50 mL glass beaker. Then add 1 mL of catalase extract and swirl gently for 10 seconds. After swirling for 10 seconds add 10 mL of H2SO4. For the other timed experiments (30,60,90,120, 180, and 360 seconds), repeat the same procedure used for the 10 second experiment except allow for the others to continue for their respected amount of time while swirling gently. Remember to remove a 5-mL and assay for the amount of...


Bibliography: Novozymes, . N.p.. Web. 19 Nov 2013.
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