Review the key concepts, formulae, and examples before starting your quiz.
🔑Concepts
Enzymes are biological catalysts made of protein molecules that speed up metabolic reactions by lowering the activation energy without being consumed in the process.
The 'Lock and Key' hypothesis states that the substrate molecule has a complementary shape to the active site of the enzyme, forming an Enzyme-Substrate Complex ( Complex).
Effect of Temperature: At low temperatures, molecules have low kinetic energy, resulting in fewer successful collisions. As temperature increases, the rate of reaction increases until it reaches the optimum temperature (usually for human enzymes).
Denaturation by Temperature: Beyond the optimum temperature, the increased thermal energy breaks the hydrogen bonds and other interactions holding the enzyme's tertiary structure. The active site changes shape, and the substrate can no longer fit.
Effect of pH: Each enzyme has an optimum (e.g., Pepsin at , Trypsin at ). Deviations from the optimum alter the ionization of amino acid R-groups, disrupting the ionic bonds that maintain the active site shape.
Irreversibility: While low temperatures only slow down reactions, extreme or high temperatures usually cause irreversible denaturation of the protein structure.
📐Formulae
💡Examples
Problem 1:
In an experiment, of starch is broken down by amylase. At , the reaction takes . At , it takes . Calculate the rate of reaction at and determine the value for this temperature range.
Solution:
- .
- .
- .
Explanation:
The rate is the reciprocal of the time taken for the substrate to disappear. The coefficient of indicates that the rate of reaction doubled with a increase in temperature, which is typical for enzyme-controlled reactions below the optimum temperature.
Problem 2:
An enzyme-controlled reaction is measured at and . The reaction proceeds rapidly at but does not occur at the other values. Identify the enzyme and explain the result.
Solution:
The enzyme is likely Pepsin. At and , the concentration of ions is too low, which disrupts the ionic bonds in the enzyme's structure, causing denaturation.
Explanation:
Pepsin is a protease found in the stomach where conditions are highly acidic ( provides ions). Enzymes are sensitive to ; if the shifts too far from the optimum, the change in charge on the amino acids causes the protein to unfold, destroying the active site.