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Biochemical Engineering

The Woolf-Augusteinsson-Hofstee plot of ν versus ν/[S] and the Eadie-Scatchard plot of ν/[S] versus ν do not involve reciprocals of ν therefore are considered to be more reliable when the error in v is

Biochemical Engineering, Enzymes And Kinetics /
Question: The Woolf-Augusteinsson-Hofstee plot of ν versus ν/[S] and the Eadie-Scatchard plot of ν/[S] versus ν do not involve reciprocals of ν therefore are considered to be more reliable when the error in v is
[A].

non-significant

[B].

significant

[C].

nothing to do with the reliability

[D].

non significant in selected cases

Answer: Option B

Explanation:

No answer description available for this question.

The Woolf-Augusteinsson-Hofstee plot of ν versus ν/[S] and the Eadie-Scatchard plot of ν/[S] versus ν do not involve reciprocals of ν therefore are considered to be more reliable when the error in v is Read More »

Biochemical Engineering, Enzymes And Kinetics

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

Biochemical Engineering, Enzymes And Kinetics /
Question: 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

Answer: Option A

Explanation:

No answer description available for this question.

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 Read More »

Biochemical Engineering, Enzymes And Kinetics

The usual method(s) to solve rate equation of simple enzyme kinetics is/are

Biochemical Engineering, Enzymes And Kinetics /
Question: The usual method(s) to solve rate equation of simple enzyme kinetics is/are
[A].

Michaelis Menten approach

[B].

Briggs-Haldane approach

[C].

Numerical solution approach

[D].

all of these

Answer: Option D

Explanation:

No answer description available for this question.

The usual method(s) to solve rate equation of simple enzyme kinetics is/are Read More »

Biochemical Engineering, Enzymes And Kinetics

Which of the following statements is true for enzymatically catalyzed reaction?

Biochemical Engineering, Enzymes And Kinetics /
Question: Which of the following statements is true for enzymatically catalyzed reaction?
[A].

The activation energy of the reaction is lowered so that a larger proportion of the substrate qualifies to overcome it

[B].

Additional substrate molecules are energized to overcome the activation energy of the reaction

[C].

The activation energy of the reaction is increased, thus decreasing the likelihood that any substrate molecules will overcome it

[D].

The activation energy of the reaction is lowered so that a fewer substrate molecules can overcome it

Answer: Option A

Explanation:

No answer description available for this question.

Which of the following statements is true for enzymatically catalyzed reaction? Read More »

Biochemical Engineering, Enzymes And Kinetics

Which of the following step is assumed to be the slowest step in the Michaelis Menten equation?

Biochemical Engineering, Enzymes And Kinetics /
Question: Which of the following step is assumed to be the slowest step in the Michaelis Menten equation?
[A].

The substrate consuming step

[B].

The product releasing step

[C].

Formation of enzyme substrate complex

[D].

None of these

Answer: Option B

Explanation:

No answer description available for this question.

Which of the following step is assumed to be the slowest step in the Michaelis Menten equation? Read More »

Biochemical Engineering, Enzymes And Kinetics

For an enzyme that displays Michaelis-Menten kinetics, the reaction velocity (as a fraction of Vmax) observed at [S] = 2 KM will be

Biochemical Engineering, Enzymes And Kinetics /
Question: For an enzyme that displays Michaelis-Menten kinetics, the reaction velocity (as a fraction of Vmax) observed at [S] = 2 KM will be
[A].

0.09

[B].

0.33

[C].

0.66

[D].

0.91

Answer: Option C

Explanation:

No answer description available for this question.

For an enzyme that displays Michaelis-Menten kinetics, the reaction velocity (as a fraction of Vmax) observed at [S] = 2 KM will be Read More »

Biochemical Engineering, Enzymes And Kinetics

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?

Biochemical Engineering, Enzymes And Kinetics /
Question: 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

Answer: Option A

Explanation:

No answer description available for this question.

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? Read More »

Biochemical Engineering, Enzymes And Kinetics