Enzymes and Kinetics MCQs

Welcome to our comprehensive collection of Multiple Choice Questions (MCQs) on Enzymes and Kinetics, a fundamental topic in the field of Biochemical Engineering. Whether you're preparing for competitive exams, honing your problem-solving skills, or simply looking to enhance your abilities in this field, our Enzymes and Kinetics MCQs are designed to help you grasp the core concepts and excel in solving problems.

In this section, you'll find a wide range of Enzymes and Kinetics mcq questions that explore various aspects of Enzymes and Kinetics problems. Each MCQ is crafted to challenge your understanding of Enzymes and Kinetics principles, enabling you to refine your problem-solving techniques. Whether you're a student aiming to ace Biochemical Engineering tests, a job seeker preparing for interviews, or someone simply interested in sharpening their skills, our Enzymes and Kinetics MCQs are your pathway to success in mastering this essential Biochemical Engineering topic.

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Enzymes and Kinetics MCQs | Page 3 of 11

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Q21.
In competitive inhibition a factor is obtained from the measurement of

a.

Vmax

b.

KM

c.

Y-intercept in Lineweaver-Burk Plot

d.

None of these

Discuss
Answer: (b).KM
Q22.
Which of these proteases is not a cysteine active site protease?

a.

Calpain

b.

Cathepsin D

c.

Papain

d.

None of the above

Discuss
Answer: (b).Cathepsin D
Q23.
Given an enzyme with a Km = 10m M and Vmax = 100 m mol/min. If [S] = 100 m M, which of the following will be true?

a.

A 10 fold increase in Vmax would increase velocity 10 fold y

b.

A 10 fold decrease in Km would increase velocity

c.

Both (a) and (b)

d.

A 10 fold increase in Vmax would decrease velocity 20 fold

Discuss
Answer: (a).A 10 fold increase in Vmax would increase velocity 10 fold y
Q24.
The conformational change in an enzyme after the substrate is bound that allows the chemical reaction to proceed, can be explained by

a.

induced fit

b.

transition

c.

fit and fine

d.

Pasteur

Discuss
Answer: (a).induced fit
Q25.
The active site of an enzyme remains

a.

at the center of globular proteins

b.

rigid and does not change shape

c.

complementary to the rest of the molecule

d.

none of the above

Discuss
Answer: (d).none of the above
Q26.
An enzyme and a reactant molecule maintain relationship as

a.

a temporary association

b.

an association stabilized by a covalent bond

c.

one in which the enzyme is changed permanently

d.

non complementary binding

Discuss
Answer: (a).a temporary association
Q27.
An enzyme is assayed at an initial substrate concentration of 2 x 10¯⁵M. In 6 minute, half of the substrate is used. The Km for the substrate is 2 x 10¯³M. The value of k in minute is

a.

0.115

b.

0.42

c.

0.093

d.

6.693

Discuss
Answer: (a).0.115
Q28.
The plot commonly used for determining the value of Vmax is

a.

Lineweaver Burk plot

b.

Langmuir plot

c.

Eadie Hofstee plot

d.

all of these

Discuss
Answer: (d).all of these
Q29.
Quasi steady state is also known as

a.

Michaelis Menten approach

b.

Briggs-Haldane approach

c.

Pseudo steady state

d.

all of the above

Discuss
Answer: (c).Pseudo steady state
Q30.
Which of these enzymes contains a Zinc (Zn) ion?

a.

Carboxypeptidase A

b.

Phosphorylase B kinase

c.

Tyrosine hydroxylase

d.

Phosphodiesterase

Discuss
Answer: (a).Carboxypeptidase A
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