Before You Begin
Question #44959
The Question
Consider the enzymatic hydrolysis of cellobiose () by the enzyme cellulase. The reaction proceeds rapidly at and , but ceases completely at . Evaluate the following six statements regarding the substrate, the enzyme, and the reaction thermodynamics:
I. Cellobiose contains a glycosidic linkage, which is a hemiacetal linkage that undergoes rapid mutarotation at , preventing enzyme recognition. II. The cessation of hydrolysis at 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 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 () at both and . 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 () of the reaction towards the formation of D-glucose at .
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
| Subject | Chemistry |
| Chapter | Biomolecules - Class 12 |
| Concept | Glycosidic Linkage Geometry |
| Difficulty | 8 |
| Cognitive Load | 7 |
| Target Solve Time | 160 sec |
| Access | Free |