The enzyme catalase is highly reactive and specialized in detoxifying body cells. It works on the basis of iron and is even more efficient when combined with other trace elements. In microbiology, it is used for preliminary differentiation of bacteria.
What is catalase?
Catalase removes toxic hydrogen peroxide (H2O2) from cells, as they would otherwise be destroyed by the aggressive oxygen compound. The enzyme breaks down hydrogen peroxide into water and oxygen, thereby rendering the chemical compound, which is dangerous to cells, harmless. This is why the fast-reacting enzyme is also called oxido-reductase (common name: CAT). Hydrogen peroxide is formed in the body as a degradation product of the enzyme superoxide dismutase, which reduces purines and oxidizes fatty acids. Catalase is one of the most effective enzymes: a single molecule is capable of breaking down up to 40 million other molecules into their components per second. Every molecule of H2O2 that reaches the active catalase center by diffusion is immediately broken down. Catalase is found in almost all animal and plant foods. It specializes in scavenging free radicals. These are oxygen-containing compounds with a free electron that are very aggressive. They either give up an electron or take one away from other compounds. This creates new free radicals.
Function, effect and tasks
In microbiological diagnostics, the enzyme is used for the preliminary classification of bacteria. With the help of the catalase reaction, scientists can distinguish between streptococci and staphylococci. The coagulase reaction is then carried out to determine the bacterial strains in more detail. Since catalase is one of the anti-oxidative enzymes, it protects the body’s cells from attack by free radicals. In particular, it breaks down harmful peroxides. In order for catalase to work optimally, it must always have enough selenium, copper and zinc available. These trace elements help the body to produce catalase itself. Thanks to its anti-inflammatory properties, the bio-catalyst can increase life expectancy by around one-fifth, as animal studies have shown. Taken as a dietary supplement, it can restore gray hair to its original color. This is because H2O2, which blocks melanin production in hair cells, is to blame for graying. In the homeopathic dosage form Catalase D30, it can also be applied externally to the hair together with bio-active carrier substances.
Formation, occurrence, properties and optimal values
Catalase is found in the peroxisomes of almost all aerobic organisms. Fungi, plants and oxygen-requiring bacteria also possess the enzyme. In humans, it is particularly concentrated in the liver, kidneys, and red blood cells. It is also integrated into the skin metabolism. Catalase has four trivalent iron porphyrin molecules (heme groups) and is composed of 526 amino acids. It forms further molecular complexes with chromium, copper and iron compounds, which also have a catalytic effect. To compensate for an existing catalase deficiency in the body, the affected person should consume corn, milk, green peas, mangoes, soybeans and honey. Alternatively, a catalase supplement is available either in the form of pure catalase or as a mixture of different antioxidants. Taken with meals, the fast-working enzyme promotes digestion. Consumed one and a half to two hours before and after meals, it has an anti-inflammatory effect.
Diseases and disorders
Catalase deficiency can lead to serious health disorders. It is considered a metabolic disease and, if genetic, is caused by mutations in the CAT gene. The hereditary disease is particularly common in Japan and manifests itself in the form of premature aging, degenerative diseases and the onset of diabetes mellitus. Akatalasemia affects a maximum of 9 out of 100,000 patients. The autosomal recessive inherited catalase deficiency occurs in people of any age group and is manifested by insufficient activity of catalase bound in red blood cells. Affected individuals usually have no symptoms. Japanese patients, on the other hand, usually also develop ulcers, diabetes and arteriosclerosis. Catalase deficiency is associated with diseases such as COPD (chronic obstructive pulmonary disease), multiple sclerosis, scleroderma, dementia and Parkinson’s disease.The so-called white spot disease (vitiligo) is also caused by too little catalase in the blood. The disease manifests itself – as the name suggests – by firmly outlined patches on the skin. According to the WHO, 1% of the world’s population suffers from vitiligo. The disease, which is psychologically very stressful for patients, is most likely hereditary. It is painless. The performance is not limited. The skin cells are discolored in the white areas due to the influence of hydrogen peroxide. Often even the hairs on them are white. The catalase deficiency first causes the skin cells to stop producing melanin (skin pigment). This happens as hydrogen peroxide forms hydroxyl free radicals that block the melanin-producing enzyme tyrosinase. They are then destroyed by the aggressive H2O2. The eye pigments are also affected. In severe disease, more than 80% of the skin surface is covered with white patches. The disease progresses in episodes and then comes to a standstill for still unexplained reasons. Sometimes only the mechanically stressed skin regions are most severely affected. Scientists suspect that vitiligo is triggered by too frequent severe sunburns, severe psychological stress, and certain heart and blood pressure medications. In otherwise healthy people, too much UV light can cause catalase concentrations in skin cells to be reduced.
