Get Detailed Information on Catalase from This Article

As a substance, catalase was first discovered in 1811 by Louis Jacques Thénard, the discoverer of hydrogen peroxide. In 1900, Oscar Loew named this enzyme capable of degrading hydrogen peroxide "catalase", and discovered that this enzyme exists in many plants and animals. In 1937, James B. Sumner crystallized catalase from bovine liver and obtained the molecular weight of the enzyme the following year. In 1969, the amino acid sequence of cattle catalase was solved. Then, in 1981, its three-dimensional structure was resolved. Catalase exists in almost all living 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 an antioxidant defense mechanism. Catalase is a new and functional enzyme preparation. Catalase is widely distributed in the biological world, almost from animals to plants, and even from humans to single-celled organisms. Catalase is a natural enemy of oxygen free radicals (reactive oxygen species, ROS) and mycotoxins (oxidizing cell membranes, proteins and nucleic acids). It is the number one killer of oxygen free radicals in the body, is the foundation of life and health, and is an active substance derived from living organisms, which can eliminate harmful substances produced by organisms in the metabolic process. Catalase is regarded as the most magical enzyme in life sciences, and the garbage cleaning machine in the human body. By continuously supplementing the body with catalase, it has the special effects of detoxification, disease resistance, liver and kidney protection, protection and repair of gastrointestinal mucosa, increase of feed intake, and prevention of cell aging. There are more than 40 kinds of enzymes in peroxisomes, and the types and proportions of oxidases contained in each peroxisome are different. But catalase is present in the peroxisomes of all cells, accounting for about 40% of the total amount of peroxisome enzymes. The functions of various peroxisomes are different, but they all have the function of oxidizing multiple substrates, catalyzing the generation and decomposition of hydrogen peroxide. In the process of oxidizing the substrate, oxidase can reduce oxygen to peroxide, and catalase can reduce hydrogen peroxide to water. Therefore, the main function of peroxisomes in liver and kidney cells is to prevent excessive production of hydrogen peroxide, so as to avoid cell poisoning and protect cells. The color of catalase is white to light brown powder, molecular weight is about 240KDa, isoelectric point is 5.2, α-helical structure, soluble in water, almost insoluble in organic solvents such as ethanol, chloroform and ether. The enzyme is ferroporinase, which contains 4 iron atoms in a molecule, and its functional group is heme. Enzymatic antioxidants are an antioxidant enzyme contained in the body itself, while non-enzymatic antioxidants are a single-line supplement. Enzymes are involved in all metabolism, so the onset and absorption of enzymes are based on the body's chemical reactions, and non-enzyme antioxidants have low bioavailability and need to be transformed in the body before they can be absorbed and utilized by the body. And most non-enzymatic antioxidants work by promoting the production of antioxidant enzymes in the body. With the same dosage of antioxidant enzymes and antioxidants, the effect of antioxidant enzymes is more than 1000 times higher than that of other antioxidants.