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🧪 Chemistry  ·  Surface Chemistry  ·  NEET & JEE

Which of these best explains why enzyme catalysis is highly specific compared to ordinary chemical catalysts?

Answer: Enzymes have a specific active site shape that fits only particular substrate molecules.

  • A Enzymes are claimed to work equally well at any temperature and pH as widely reported
  • B Enzymes have a specific active site shape that fits only particular substrate molecules
  • C Enzymes are in fact usually simple inorganic compounds rather than proteins in standard practice
  • D Enzymes act by directly raising the temperature of the reaction mixture under most conditions encountered

Correct answer: B. Enzymes have a specific active site shape that fits only particular substrate molecules

Explanation: The lock-and-key fit between an enzyme active site and its specific substrate explains why enzyme catalysis is far more specific than typical catalysts.

Adsorption Isotherm: x/m vs PressureP (pressure)x/mlow P: x/m ∝ Phigh P: saturation plateauAt high pressure, all surface sites are occupied - the curve flattens (monolayer saturation)

A typical adsorption isotherm: x/m (mass adsorbed per gram of adsorbent) rises steeply at low pressure, then flattens into a saturation plateau as the adsorbent surface fills up.

Concept context

Explore the chemistry that happens at interfaces, from catalysts that speed up industrial reactions to colloids like milk, smoke, and gels that surround us every day.

Read the full Surface Chemistry notes →