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NCERT Exemplar · Q40

Q.The activation energy for the acid catalysed hydrolysis of sucrose is 6.22 kJ mol−1^{-1}, while the activation energy is only 2.15 kJ mol−1^{-1} when hydrolysis is catalysed by the enzyme sucrase. Explain.

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The enzyme sucrase lowers the activation energy barrier for sucrose hydrolysis from 6.22 kJ mol⁻¹ to 2.15 kJ mol⁻¹ by providing an alternative reaction pathway through an enzyme–substrate complex, making the reaction dramatically faster at biological temperatures.


The question asks you to explain why the activation energy (EaE_a) for sucrose hydrolysis drops so sharply when the catalyst changes from an acid (H⁺) to the enzyme sucrase. The numbers themselves are striking: 6.22 kJ mol⁻¹ vs 2.15 kJ mol⁻¹ — a reduction of about 65%. That is not a small tweak; it is a fundamental change in how the reaction proceeds.

Let’s first recall what activation energy means. It is the minimum energy that reactant molecules must possess for a collision to result in a reaction. A lower EaE_a means a much larger fraction of molecules have enough energy at a given temperature, so the rate constant kk increases exponentially (Arrhenius equation: k=Ae−Ea/RTk = A e^{-E_a/RT}). So the enzyme makes the reaction happen millions of times faster than the acid-catalysed version under the same conditions.

Now, why does this happen?

  1. Acid catalysis works by brute force. In the acid-catalysed hydrolysis, H⁺ ions (from a strong acid like HCl) protonate the glycosidic oxygen in sucrose. This makes the C–O bond more polar and easier to break. But the transition state — the highest-energy, most unstable arrangement along the reaction coordinate — still involves a highly strained, high-energy species. The acid simply lowers the barrier a bit by stabilising the protonated intermediate, but the pathway remains essentially the same as the uncatalysed reaction, just with a slightly lower hill to climb.

  2. Enzyme catalysis creates a completely new path. Sucrase (also called invertase) is a protein with an active site that binds the sucrose molecule in a precise orientation. The binding itself is not just a passive grip — it involves multiple non-covalent interactions (hydrogen bonds, van der Waals forces, hydrophobic effects) that distort the sucrose molecule toward its transition-state geometry. This is called transition-state stabilisation. The enzyme’s active site is complementary to the transition state, not to the reactant sucrose. So as the substrate binds, the enzyme strains bonds and positions catalytic groups (often acidic/basic amino acid side chains) to directly participate in bond breaking and forming.

  3. The enzyme provides a lower-energy alternative route. Instead of going over the same high hill as the acid-catalysed reaction, the enzyme–substrate complex (ES) proceeds through a series of intermediates (e.g., a covalent glycosyl-enzyme intermediate) that are each much lower in energy than the acid-catalysed transition state. The activation energy of 2.15 kJ mol⁻¹ corresponds to the highest barrier along this new, multi-step pathway — which is far lower than the single-step barrier in the acid-catalysed case.

Tip

A useful mental picture: acid catalysis is like climbing a steep hill with a walking stick; enzyme catalysis is like finding a tunnel through the hill. Both get you to the other side, but the tunnel is far easier.

  1. The entropy factor also matters. In the acid-catalysed reaction, two separate species (sucrose and water) must come together in the correct orientation for hydrolysis — this costs entropy. In the enzyme-catalysed reaction, the substrate is held in the active site with water already positioned nearby, so the entropic cost is largely prepaid by the binding step. This further lowers the free energy of activation (ΔG‡\Delta G^\ddagger), which is what the experimental EaE_a reflects when measured from the temperature dependence of the rate. …

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