Question

While studying enzyme kinetics in the lab, a scientist observed that the rate of a reaction involving enzyme amylase increased as the concentration of starch increased. With further increase in starch concentration, the amylase activity did not change. Why did this happen?



The starch molecules did not bind to the enzyme amylase efficiently.



The enzyme amylase was saturated, as all its active sites were occupied by substrate starch.



The starch molecules were converted to product glucose as soon as they bound to enzyme amylase.

Answer 1

From the question, we can conclude that the concentration of the enzyme is constant while there is an increase in the concentration of substrate.



From the diagram you can see that as the conc. of starch increases, the rate of reaction of the enzyme will also increase until a certain point where it will plateau. This is because at that particular point all enzymes are at their maximum activities.

So, according to the diagram and the information provided, what according to you is the answer?

Answer 2

im not getting it.

Answer 3

b?

Answer 4

Yups, it's b. As increasing the conc. of substrate while keeping the conc. of enzyme constant will cause the active sites to be all occupied at a certain point.

Answer 5

K. Thanks..i undertsnad now. lol

Answer 6

Okay :)

Answer 7

you're welcome by the way :)

Answer 8

Funny side note:
Experiments actually show (at least in the lab I am in now) that MM-kinetics like to take the following curve when we go into a huge substrate concentration.