Catalase is said to be a common enzyme which is found almost in all living organisms that are exposed to oxygen. For example: animals, fruits or vegetables. Catalase catalyzes the decomposition of hydrogen peroxide to oxygen and water. Catalase has four iron groups, which allow catalase to act with hydrogen peroxide. Each and every enzyme has their own optimum pH, which is the most favorable condition for them to work. Enzymes speed up the reaction rate (catalysis) or slower the reaction rate (catalysis) at a particular pH. Thus the laboratory result shows that the most favorable pH for catalase is pH 7 (Toone and Nord, 2011). The results have few practical applications in biological systems, real life and in industries. Catalase is used for quality control and analysis. For example: catalase is used in textile industry, also to check and control milk quality and also used in cosmetic industry, like: for dace mask. Other applications include production of baked goods and beverages. The genetically modified bacterial and fungal cultures (Aspergilla) can produce catalase that is used in food manufacturing industries (Koleva et al., 2008). The quantity of catalase inside the cells of microorganisms depends upon the medium applied to culture cells and the cell growth condition. Catalase alone or with glucose oxidase is used as preserving system. It is used to preserve egg products and mayonnaise, for example: dried egg or milk and cheese preparation. Catalase prevents the accumulation of hydrogen peroxide inside human system and thus stops the process of graying hair.
Koleva, D., Petrova, V., Hristozova, T. and Kujumdzieva, A. (2008). Study of Catalase Enzyme in Methylotrophic Yeasts. Biotechnology & Biotechnological Equipment, 22(2), pp.762-768.
Toone, E. and Nord, F. (2011). Advances in enzymology. Hoboken, N.J.: Wiley.
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