Catalase is an enzyme that can catalyze the decomposition of hydrogen peroxide into oxygen and water and is present in the chloroplasts, mitochondria, endoplasmic reticulum, liver and red blood cells of plants.
Catalase is an antioxidant enzyme that is ubiquitous in all organisms. It is a tetramer (a type of protein) with four polypeptide chains, each containing more than 500 amino acids. It consists of four iron-based (porphyrin heme) reactive with hydrogen peroxide. Catalase is the power house of the enzyme world, which is the highest conversion rate of all enzymes (millions of hydrogen peroxide molecules can be converted to water and oxygen with just one molecule!) and has dozens of vital functions. Moreover, this fantastic enzyme is an extremely important enzyme in all fields. In this article, we will investigate more about catalase and study how this vital enzyme can be used in various industries.
Brief introduction
Catalase is an enzyme that catalyzes the decomposition of hydrogen peroxide into oxygen and water and is present in the chloroplasts, mitochondria, endoplasmic reticulum, liver and red blood cells of plants. It is a peroxidase labeling enzyme that accounts for about 40% of total peroxidase. Catalase is present in all tissues of all known animals, especially in high concentrations of liver. And it is used in the food industry to remove hydrogen peroxide from milk used to make cheese. It is also used in food packaging to prevent food from being oxidized.
What does catalase do?
Essentially, the key role of catalase is the decomposition of hydrogen peroxide. This makes it very easy to detect the presence of catalase in tissue samples and microbial samples. When hydrogen peroxide is added to the sample containing catalase, a visible reaction occurs, demonstrating its presence. There are dozens of practical applications in various industries and fields, including:
If you like your cheese, thanks to catalase! Hydrogen peroxide must be removed before changing certain types of cheese from milk to cheese. It is used in certain varieties such as Swiss cheese because hydrogen peroxide has the same effect as pasteurization without the need for pasteurization of milk. This heat kills many natural cheese enzymes, which is essential for the development of the flavor of Swiss cheese and its similar products. However, hydrogen peroxide is toxic to humans and must therefore be removed by the addition of catalase. Catalase is also used in food packaging to prevent food from being oxidized.
Some contact lens cleaners use hydrogen peroxide, which must be removed before returning it to the eye. Therefore, catalase is the second most important step in the cleaning process of contact lenses. After soaking the glass in a hydrogen peroxide-containing detergent, the residual hydrogen peroxide is removed with catalase before use. In recent years, catalase has been used in the beauty industry. Some skin care products have been added with catalase and hydrogen peroxide to increase the cellular oxygen content in the upper epidermis.
Catalase is very important to the work of microbiologists. It is used to identify bacterial species because its presence (detected by the addition of hydrogen peroxide and subsequent reactions) or absence indicates the presence of different types of bacteria. Some organisms are catalase-positive (staphylococcus and micrococci) and some are catalase-negative (streptococci and enterococci). This is very helpful for medical research and diagnosis.
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