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Catalase (CAT), an enzyme that catalyzes the breakdown of hydrogen peroxide into oxygen and water, is present in the peroxides of cells. Catalase is a marker enzyme of peroxidase bodies, accounting for about 40% of the total peroxidase bodies. Catalase is present in all known animal tissues, especially in high concentrations in the liver. Catalase is used in the food industry to remove hydrogen peroxide from milk used to make cheese. Catalase is also used in food packaging to prevent food from being oxidized.
Catalase is present in almost all organisms. It is commonly found in breathing organisms, mainly in plant chloroplasts, mitochondria, endoplasmic reticulum, animal liver and red blood cells, and its enzymatic activity provides the body with antioxidant defense mechanism.
CAT is a red blood enzyme with different structures from different sources. The activity level varies in different tissues. Hydrogen peroxide breaks down faster in the liver than in organs such as the brain or heart because of the high levels of CAT in the liver.
Catalase is used in the food industry to remove hydrogen peroxide from milk used to make cheese. Catalase is also used in food packaging to prevent food from being oxidized. In the textile industry, catalase is used to remove hydrogen peroxide from fabrics to ensure that the finished product is free of peroxide. It is also used to clean contact lenses: after the glasses have been soaked in a detergent containing hydrogen peroxide, catalase is used to remove the residual hydrogen peroxide before use. Use of catalase in the beauty industry: some facials incorporate the enzyme and hydrogen peroxide to increase the oxygen content of cells in the upper layers of the epidermis.
Catalase is also often used in the laboratory as a tool to understand the effect of enzymes on reaction rates.