Jonathan Khan October 3, 2010

Ms. Crowley Catalase Lab Essays

Product Formed
0.9
0.8
0.7
0.6
0.5 Product Formed

0.4
0.3
0.2
0.1
0
Time
1.
a. The initial rate of the enzyme reaction is .025 mg of product formed per second

b. The rate of enzymatic activity at fifty seconds is .005 mg of product per second

i. At this point, all molecules of enzyme are bound to a molecule of

substrate, and are working at full capacity causing the rate of the reaction

to slow down at this point.

c. The effect on product formation if the enzyme were heated to a temperature of

100° C for ten minutes before repeating the experiment would be that there would

be little to no product formation.

i. This is because the heating of the enzyme will cause it to denature (change

shape). At this point, the shape of the active site will no longer be able to

conform to the shape of the substrate, thus preventing a reaction.

d. Altering the substrate concentration will affect the rate of the reaction positively,

but only up to a certain point.

 i. If substrate is added to an enzyme – substrate solution, the rate of

enzymatic activity will increase only up to a point where each molecule of

enzymes is bound to and acting on a molecule of substrate. At this point,

the rate of the reaction will slow down, and eventually flat line at this

point.

e. Altering the pH will affect the rate of the reaction negatively.

i. When an enzyme is placed outside of its normal operating environment

(pH of 7), it stops working. This is due to the enzyme denaturing and no

longer being functional.

2. The lock and key theory of enzyme substrate interactions is the current theory used to

explain how enzymes work. One specific example of this theory is the complex of lactose

and lactase. Where lactose is the substrate and lactase is the enzyme. When lactase comes

into contact with lactose, it positions itself so that lactose can fit into the active site of the

enzyme. The active site is formed by the interactions of functional (R) groups on the

amino acid chain(s). Many things can affect the rate of enzymatic action. Four of these

things are; substrate concentration, a shift in pH, a shift in temperature, and competitive

inhibition. Substrate concentration affects the rate of enzymatic activity in the way that

the rate of enzymatic activity will increase only up to a point where each molecule of

enzymes is bound to and acting on a molecule of substrate. At this point, the rate of the

reaction will slow down, and eventually flat line at this point. By shifting the pH of the

environment that the enzyme is working in, the rate of activity slows down. Most

enzymes work best at a neutral pH of 7. If the pH is shifted too greatly, the enzyme will
 become denatured, meaning that the shape of the enzyme has changes, causing the active

site’s shape to change, rendering the enzyme unable to fit with its substrate. Thus forth

causing no reaction. A shift in temperature will affect the reaction in two ways. If

temperature is increased, the rate of activity will increase due to an increase in kinetic

energy which causes an increase in the number of effective collisions. After a few

degrees, the enzyme will denature due to a shift too far outside of its operating range,

causing the reaction to decrease in rate. However, a decrease in temperature will not

cause an enzyme to denature, all it will do is cause a decrease in kinetic energy, causing

less effective collisions, and causing the rate of the reaction to slow down. Competitive

inhibition will negatively impact the rate of enzyme activity; this is due to the fact that a

substance other than the substrate has attached itself to the active site of an enzyme. This

prevents the substrate from attaching to the active site of the enzyme, causing the reaction

to slow down. In humans this can be fatal; an example of this is cyanide poisoning. The

cyanide molecule attaches itself irreversibly to the active sites of respiratory enzymes,

causing death within minutes.

6. In order to test the effect of varying pH on the rate of enzymatic activity, a controlled

experiment is necessary. Most of the materials used int eh lab can be used to test the

effect of a variable pH. Instead of varying