Ib Bio Experiment on Effect of Substrate Conc on Enzyme Activity
Practical Assessment 2 – The effect of substrate concentration on the rate of enzyme activity of Catalase
Aim
To investigate the effect of substrate concentration (manipulated by increasing concentration of hydrogen peroxide) on the rate of enzyme activity of catalase, produced by liver cells, on the decomposition of hydrogen peroxide.
Introduction
Enzymes are biological catalysts that increase the rates of reactions. In an enzyme-catalyzed reaction, the substrate binds to the active site and forms enzyme-substrate complex with the enzyme through the lock and key method (where the lock represents the enzyme and the key represents the substrate). The enzyme then breaks the bonds in the substrate. The product of the reaction then leaves the enzyme, which remains unchanged after the reaction. Without enzymes, many essential processes, such as digestion, would occur too slowly for life to continue.
Catalase is an enzyme produced by our liver cells to break down hydrogen peroxide – a common end product of metabolism, but highly toxic to tissues if accumulated in the body – into water and oxygen.
The equation of the reaction is as follows:
2 H2O2 O2 + 2 H2O
Catalase
Catalase
In this experiment, we obtain 6% hydrogen peroxide solution from a pharmacy and extract equal concentrations of catalase from liver cells. Filter paper discs are dipped into the catalase solution before they are submerged in hydrogen peroxide solution. The oxygen produced from the enzyme reaction will form on the discs and cause the disc to be buoyant enough to float upwards. We can investigate the effects of substrate concentration on the rate of reaction by catalase by using different concentrations of hydrogen peroxide solution, and measuring the rate of reaction by measuring time taken for the disc to float to the surface when sufficient oxygen is produced.
Hypothesis
The hypothesis for this experiment is that the rate of
Aim
To investigate the effect of substrate concentration (manipulated by increasing concentration of hydrogen peroxide) on the rate of enzyme activity of catalase, produced by liver cells, on the decomposition of hydrogen peroxide.
Introduction
Enzymes are biological catalysts that increase the rates of reactions. In an enzyme-catalyzed reaction, the substrate binds to the active site and forms enzyme-substrate complex with the enzyme through the lock and key method (where the lock represents the enzyme and the key represents the substrate). The enzyme then breaks the bonds in the substrate. The product of the reaction then leaves the enzyme, which remains unchanged after the reaction. Without enzymes, many essential processes, such as digestion, would occur too slowly for life to continue.
Catalase is an enzyme produced by our liver cells to break down hydrogen peroxide – a common end product of metabolism, but highly toxic to tissues if accumulated in the body – into water and oxygen.
The equation of the reaction is as follows:
2 H2O2 O2 + 2 H2O
Catalase
Catalase
In this experiment, we obtain 6% hydrogen peroxide solution from a pharmacy and extract equal concentrations of catalase from liver cells. Filter paper discs are dipped into the catalase solution before they are submerged in hydrogen peroxide solution. The oxygen produced from the enzyme reaction will form on the discs and cause the disc to be buoyant enough to float upwards. We can investigate the effects of substrate concentration on the rate of reaction by catalase by using different concentrations of hydrogen peroxide solution, and measuring the rate of reaction by measuring time taken for the disc to float to the surface when sufficient oxygen is produced.
Hypothesis
The hypothesis for this experiment is that the rate of