Enzyme Kinetics MCQ Quiz in தமிழ் - Objective Question with Answer for Enzyme Kinetics - இலவச PDF ஐப் பதிவிறக்கவும்

Last updated on Apr 10, 2025

பெறு Enzyme Kinetics பதில்கள் மற்றும் விரிவான தீர்வுகளுடன் கூடிய பல தேர்வு கேள்விகள் (MCQ வினாடிவினா). இவற்றை இலவசமாகப் பதிவிறக்கவும் Enzyme Kinetics MCQ வினாடி வினா Pdf மற்றும் வங்கி, SSC, ரயில்வே, UPSC, மாநில PSC போன்ற உங்களின் வரவிருக்கும் தேர்வுகளுக்குத் தயாராகுங்கள்.

Latest Enzyme Kinetics MCQ Objective Questions

Top Enzyme Kinetics MCQ Objective Questions

Enzyme Kinetics Question 1:

In an enzyme-catalysed reaction

\( \mathrm{E}+\mathrm{S} \underset{k_{-1}}{\stackrel{k_1}{\rightleftharpoons}} \mathrm{ES} \stackrel{k_2}{\longrightarrow} \mathrm{E}+\mathrm{P} \)

\(k_2=3.42 \times 10^4 \mathrm{~s}^{-1} . \text { If }[E]_0\) = \(1 \times 10^{-2} \mathrm{~mol} \mathrm{dm}^{-3} \),  the magnitude of maximum velocity and turnover number using Michaelis-Menten kinetics are

  1. \(3.42 \times 10^2 \mathrm{~mol}\ \mathrm{dm}^{-3} \mathrm{~s}^{-1} ; \) \(3.42 \times 10^4 \mathrm{~s}^{-1}\)
  2. \(3.42 \times 10^6 \mathrm{~mol}\ \mathrm{dm}^{-3} \mathrm{~s}^{-1} ;\) \( 3.42 \times 10^4 \mathrm{~s}^{-1}\)
  3. \(3.42 \times 10^4 \mathrm{~mol}\ \mathrm{dm}^{-3} \mathrm{~s}^{-1} ; \) \(3.42 \times 10^6 \mathrm{~s}^{-1}\)
  4. \(3.42 \times 10^4 \mathrm{~mol}\ \mathrm{dm}^{-3} \mathrm{~s}^{-1} ;\) \( 3.42 \times 10^2 \mathrm{~s}^{-1}\)

Answer (Detailed Solution Below)

Option 1 : \(3.42 \times 10^2 \mathrm{~mol}\ \mathrm{dm}^{-3} \mathrm{~s}^{-1} ; \) \(3.42 \times 10^4 \mathrm{~s}^{-1}\)

Enzyme Kinetics Question 1 Detailed Solution

Concept:

  • For enzyme-catalyzed reactions that follow a Michaelis-Menten mechanism, the relationship between the rate of reaction and enzyme-substrate is given by:

\(\frac{1}{v}=\frac{1}{v_{max}}+\frac{k_M}{v_{max}}\frac{1}{[S]}\)

  • The expression has the form of a straight-line graph.

F2 Savita Teaching 30-3-23 D1

  • If we plot pf 1/v against 1/[S]. should give a gradient of KM/Vmax and an intercept of Vmax.

Explanation:-

\(\gamma_{\max }=k_2[E]_0\) = \(3.42 \times 10^4 \times 1 \times 10^{-2}\) = \(3.42 \times 10^2 \mathrm{~mol}\ \mathrm{dm}^{-3} \mathrm{sec}^{-1} \)

And T.O.N. = \(k_2=3.42 \times 10^4 \mathrm{~s}^{-1}\)

Conclusion:-

Correct option is (a)

Enzyme Kinetics Question 2:

Curding from milk, an enzyme-catalysed reaction, is most efficient around

  1. 0°C and pH ≥ 10
  2. 0°C and pH ≤ 4
  3. 0°C and 4 ≤ pH ≤ 10
  4. 25°C and 4 ≤ pH ≤ 10

Answer (Detailed Solution Below)

Option 4 : 25°C and 4 ≤ pH ≤ 10

Enzyme Kinetics Question 2 Detailed Solution

Concept:

→ The curding of milk is a complex process that involves the coagulation of milk proteins, primarily casein, by the action of enzymes called proteases.

→ The most important proteases involved in milk curdling are chymosin and pepsin, which are produced in the stomachs of young mammals to aid in the digestion of milk.

Explanation:

The efficiency of enzyme-catalyzed reactions, such as milk curdling, is affected by a number of factors, including temperature and pH. The optimal conditions for milk curdling are around 25°C and a pH between 4 and 10. 

  1. Temperature: Enzymes work best at their optimal temperature, which is the temperature at which they have the highest activity. For chymosin and pepsin, the optimal temperature is around 25°C. At higher temperatures, the enzymes become denatured, meaning their three-dimensional structure is disrupted and they lose their catalytic activity.

  2. pH: Enzymes are also sensitive to pH, which can affect their activity and stability. Chymosin and pepsin work best at a slightly acidic pH, between 4 and 5.5. However, they can also function at a pH as high as 10, although their activity is lower at this pH. The pH of milk is typically around 6.5, so acidification of milk is often required to achieve the optimal pH for curdling.

Conclusion: The most efficient conditions for milk curdling are around 25°C and a pH between 4 and 10 because these conditions provide the optimal temperature and pH for the activity of the proteases involved in the process.

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