Question:

Given below are two statements:
Statement I: Increase in temperature of a reaction mixture up to an optimum value increases the rate of enzyme reaction as it enhances the rate of collision between the substrate and enzyme active sites
Statement II: Increase in the temperature beyond an optimum value breaks the non-covalent bonds in enzyme first and thereby reaction velocity is decreased
In the light of the above statements, choose the most appropriate answer from the options given below

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Enzyme-Temperature Profile: Bell-shaped curve. Rising phase = Increased kinetic collisions. Falling phase = Thermal denaturation of tertiary structure non-covalent bonds.
  • Both Statement I and Statement II are true
  • Both Statement I and Statement II are false
  • Statement I is true but Statement II is false
  • Statement I is false but Statement II is true
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The Correct Option is A

Solution and Explanation


Step 1: Understanding the Concept:

Enzyme thermal kinetics reflect the interplay between kinetic activation energy ($Q_{10} \approx 2$) and conformational thermal denaturation.

Step 2: Detailed Explanation:

1. Statement I: As temperature rises up to the optimum temperature ($T_{\text{opt}} \approx 37-40^\circ\text{C}$ in mammals), increased thermal kinetic energy accelerates molecular motion, increasing the frequency and energy of productive collisions between substrate and catalytic active sites (doubling rate per $10^\circ\text{C}$ rise). Hence, Statement I is true.
2. Statement II: Beyond the optimum temperature, excessive thermal vibrational energy disrupts weak non-covalent interactions (hydrogen bonds, ionic bonds, hydrophobic forces) stabilizing the enzyme's native tertiary conformation, causing active site denaturation and loss of catalytic velocity. Hence, Statement II is true.

Step 3: Final Answer:

Thus, Both Statement I and Statement II are true, matching option (A).
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