Understanding The Function Of An Enzyme Biology Essay

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In this experiment, Enzyme Catalysis you should understand the function of an enzyme. An enzyme is proteins produced by living cells; they act as catalysts in biochemical reactions. An enzymes (E) activity will be greater working at a lower temperature. When an enzyme is at work it binds with a substrate(S), as a result of this binding the energy formed is the product (P).The site at where this all happens is call the active site.

E+S→ES→E+P

Many molecules other than a substrate may interact with an enzyme. If the molecule increases the rate of the reaction it is an activator, and if it decreases the rate it is an inhibitor. The enzyme used in this lab is Catalasis. Catalasis will help with the decomposition of hydrogen peroxide (H2O2).

2 H2O2→2 H2O2 + O2 (gas)

In this experiment the disappearance of the substrate H2O2 by a mixture of catalase, H2O2, sulfuric acid (H2SO4), and potassium permanganate (KMnO4).

5 H2O2 + 2 KMnO2 +3 H2SO4→ K2SO4 + 2 MnSO4 + 8 H2 + 5O2

Materials and Methods

Graduated cylinder

Gloves

Catalase, to be stored in an ice bucket

1.5% H2O2

2% KMnO2

1M H2SO4

H20

Droppers

Syringes

27 15mL cups

Stop watch

Burette

Experiments 1

Put 10 mL of 1.5% H2O2 into a clean 15mL cup

Add 1 mL of H2O

Add 10 mL of H2SO4

Mix well

Remove a 5 mL sample and place in another 15 mL cup. Place it over a white piece of paper. Us the syringe to add KMnO2 a drop at a time to the solution until a persistent pink or brown color is shown. Mix as u add each drop. Record your readings in Table 1.1

Table 1.1 Base Line Calculations

Final reading of syringe: mL

Initial Reading of syringe: mL

Base Line (Final - Initial): mL

Experiment 2

To determine the spontaneous conversion of H2O2 to H20 and O2 in an uncatalyized reaction, put a small quantity of 1.5% H2O2 (about 15ml) into a cup. Store it uncovered at room temperature for 24 hour. Repeat steps 2-5 from experiment 1 to determine the amount of H2O2 remaining. Record in Table 2.1.

Table 2 Uncatalyzed H2O2 Decomposition

Final Reading of Syringe: mL

Initial Reading of Syringe: mL

Amount of KMnO4 titrant: Ml

Amount of H2O2 spontaneously decomposed

(ML baseline-mL KMnO4): mL

Experiment 3

To determine the course of an enzymatic reaction, you will need to measure how much substrate is disappearing over time. You will measure the amount of substrate decomposed after 10, 30, 60, 90, 120, 180, and 360 seconds.

Put 10 mL of 1.5% H2O2 in a clean cup

Add 1 mL of catalase

Swirl for 10 seconds

At 10 seconds, add 10 ml of H2SO4

Repeat steps for 30, 60, 90, 120, 180, and 360 seconds

Remove a 5 mL sample and place in another 15 mL cup. Place it over a white piece of paper. Us the syringe to add KMnO2 a drop at a time to the solution until a persistent pink or brown color is shown. Mix as u add each drop. Record your readings in Table 3.1

Table 3 Experiment 3 results

KMnO4 (mL)

 

 

Time in seconds

 

10

30

60

90

120

180

360

 

 

abase Line

 

 

 

 

 

 

 

 

b:Final

 

 

 

 

 

 

 

 

c:Initial

 

 

 

 

 

 

 

 

d: b-c

 

 

 

 

 

 

 

 

e: a-d

 

 

 

 

 

 

 

 

Results

Table 1.1 Base Line Calculations

Final reading of syringe: 1.35 mL

Initial Reading of syringe: 5 mL

Base Line (Final - Initial): 3.65 mL

Table 2 Uncatalyzed H2O2 Decomposition

Final Reading of Syringe: 4 mL

Initial Reading of Syringe: 10 mL

Amount of KMnO4 titrant: 6 mL

Amount of H2O2 spontaneously decomposed

(mL baseline-mL KMnO4): 2.35 Ml

Table 3 Experiment 3 results

KMnO4 (mL)

 

 

Time in seconds

 

10

30

60

90

120

180

360

 

 

a: Base Line

3.35

3.65

3.65

3.65

3.65

3.65

3.65

 

b:Final

2.2

3.2

3.4

3.7

2.8

2.4

2

 

c:Initial

5

5

5

5

5

5

5

 

d: b-c

-2.8

-1.8

-1.6

-1.3

-2.2

-2.6

-3

 

e: a-d

6.15

5.45

5.25

4.95

5.85

6.25

6.65

 

Discussion

Table 3 showed how much the reaction changed in the course of an enzyme reaction. The Activation energy did take place, which is also called free energy of activation), the amount of energy that reactants must absorb before a chemical reaction will start. The longer the solution had to sit the longer the reaction took, but it reached a point where it dropped off. For experiment 2 it showed no matter how long it sat you would still end up with the same results, because hydrogen peroxide will work just as good no matter how old it is, because no light or other substance will reach it.

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