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Question #44959

Difficulty: 8/10 | 🟢 Free

The Question

Consider the enzymatic hydrolysis of cellobiose (\ceC12H22O11\ce{C12H22O11}) by the enzyme cellulase. The reaction proceeds rapidly at 298 K298\text{ K} and pH=5.0\text{pH} = 5.0, but ceases completely at 360 K360\text{ K}. Evaluate the following six statements regarding the substrate, the enzyme, and the reaction thermodynamics:

I. Cellobiose contains a β(1→4)\beta(1 \rightarrow 4) glycosidic linkage, which is a hemiacetal linkage that undergoes rapid mutarotation at 360 K360\text{ K}, preventing enzyme recognition. II. The cessation of hydrolysis at 360 K360\text{ K} is primarily due to the endothermic disruption of non-covalent interactions (e.g., hydrogen bonding, hydrophobic effects) within cellulase, altering its tertiary structure. III. The 'Lock and Key' specificity is lost at 360 K360\text{ K} because the thermal energy exceeds the activation energy for the cleavage of the enzyme's primary peptide bonds. IV. The hydrolysis of cellobiose into two molecules of D-glucose is thermodynamically spontaneous (ΔG<0\Delta G < 0) at both 298 K298\text{ K} and 360 K360\text{ K}. V. In the most stable chair conformation of the major product formed upon hydrolysis (in aqueous equilibrium), all hydroxyl groups and the hydroxymethyl group occupy equatorial positions. VI. Cellulase acts by lowering the activation energy of the hydrolysis, which simultaneously shifts the equilibrium constant (KeqK_{eq}) of the reaction towards the formation of D-glucose at 298 K298\text{ K}.

How many of the above statements are CORRECT?

Options

  • A.

    2

  • B.

    3

  • C.

    4

  • D.

    5

Check Your Answer

Correct Answer

Step-by-Step Solution

Explanation

How the Examiner Thinks

Mechanism_Trap

Don't get tricked by the process! Learn the mechanical traps used in competitive exam questions.

Concepts Behind This Question

Glycosidic Linkage Geometry|Enzyme Specificity 'Lock and Key'|Protein Denaturation Specificity

Why This Question Is Tricky

Common Mistakes

The question tests the critical distinction between substrate stereochemistry, thermodynamic spontaneity, and enzyme structural integrity.

A common student trap is assuming that high temperatures cause the substrate's glycosidic bond to mutarotate (confusing acetals with hemiacetals) or that the reaction becomes thermodynamically non-spontaneous.

Another trap is confusing protein denaturation (unfolding via disruption of weak forces) with degradation (cleavage of covalent peptide bonds).

The 'Lock and Key' mechanism fails here not because the 'key' (substrate) changes shape, but because the 'lock' (enzyme active site) melts thermodynamically.

Quick Facts About This Question

Question Information

SubjectChemistry
ChapterBiomolecules - Class 12
ConceptGlycosidic Linkage Geometry
Difficulty8
Cognitive Load7
Target Solve Time160 sec
AccessFree