Initially, more substrate molecules increase enzyme-substrate complex formation. Once all active sites become occupied, the reaction reaches maximum velocity (Vmax).
Low temperature decreases molecular motion and collision frequency. The enzyme usually regains normal activity when returned to its optimum temperature.
High temperature disrupts hydrogen bonds and other weak interactions responsible for maintaining enzyme structure, causing denaturation and loss of catalytic function.
Every enzyme has an optimum temperature where catalytic activity is highest. Above this temperature, the enzyme's three-dimensional structure begins to lose stability.
As temperature rises toward the optimum, enzyme and substrate molecules move faster, increasing successful collisions and enzyme-substrate complex formation. Denaturation usually occurs only above the optimum temperature.
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