Enzymology & Thermodynamics

In the presence of an enzyme, the reaction runs in the same direction as it would without the enzyme, just more quickly. For example, carbonic anhydrase catalyses its reaction in either direction depending on the concentration of its reactants. The rate of a reaction is dependent on the activation energy needed to form the transition state which then decays into products. Enzymes increase reaction rates by lowering the energy of the transition state. First, binding forms a low energy enzyme-substrate complex (ES). Secondly the enzyme stabilises the transition state such that it requires less energy to achieve compared to the uncatalyzed reaction (ES‡). Finally the enzyme-product complex (EP) dissociates to release the products.

  • Catalytic mechanisms of enzymes
  • Enzyme-substrate complex
  • Transition state of enzymes
  • Transformation of substrate
  • Production of intracellular components
  • Production of extracellular metabolites
  • Production of biomass
  • Product recovery
  • Enzymes in food digestion
  • Applications of immobilized enzymes in food
  • Single cell protein

Related Conference of Enzymology & Thermodynamics

Enzymology & Thermodynamics Conference Speakers