Catalase Powder CAS 9001-05-2

Catalase powder (CAT), molecular formula C9H10O3, CAS 9001-05-2, It is an enzyme that catalyzes the decomposition of hydrogen peroxide into oxygen and water, and exists within the peroxidase system of cells. Catalase is a marker enzyme of peroxisomes, accounting for approximately 40% of the total peroxisome enzymes. Catalase is present in various tissues of all known animals, particularly at 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. Almost all living organisms have catalase. It is widely present in respiratory organisms, mainly in chloroplasts, mitochondria, endoplasmic reticulum of plants, liver and red blood cells of animals, and its enzymatic activity provides an antioxidant defense mechanism for the body. CAT is a heme enzyme with different structures depending on its source. The level of activity varies in different organizations. Hydrogen peroxide decomposes faster in the liver than in organs such as the brain or heart, due to the high levels of CAT in the liver.

 

Hydrogen peroxide (H2O2), also known as hydrogen peroxide, has one more oxygen atom (0) than water (H2O). This oxygen atom is extremely unstable and always wants to take another oxygen atom from other molecules to form O2. We usually use hydrogen peroxide for sterilization and disinfection because bacteria are destroyed by H2O2 and die. The foaming during disinfection is the result of producing oxygen. However, hydrogen peroxide can penetrate most cell membranes, making it more cytotoxic than superoxide anion radicals (which cannot penetrate cell membranes). After penetrating the cell membrane, it can react with iron inside the cell to generate hydroxyl radicals. Catalase powder (CAT) is an important member of the antioxidant enzyme system, also known as a peroxidase, which is a binding enzyme with iron porphyrin as a secondary group.

 

SOD enzyme dismutates oxygen free radicals to produce hydrogen peroxide (H2O2) and oxygen (O2). Hydrogen peroxide remains a toxic oxidant in the body, and the function of catalase is to promote the decomposition of hydrogen peroxide into molecular oxygen and water, thus protecting cells from the toxicity of H2O2. The mechanism of CAT acting on hydrogen peroxide is essentially the dismutation of hydrogen peroxide, which requires two H2O2 molecules to meet and collide with CAT at the active center in order for the reaction to occur. The higher the concentration of H2O2, the faster the decomposition rate. Almost all physiological organisms have catalase.

 

It is widely present in respiratory organisms, mainly in chloroplasts, mitochondria, endoplasmic reticulum of plants, as well as in liver and red blood cells of animals. Its enzymatic activity provides an antioxidant defense mechanism for the body. The biological function of catalase is to promote the decomposition of hydrogen peroxide in cells, so that it does not further produce highly toxic hydroxyl radicals, thereby protecting the function of the antioxidant enzyme system. It is also of great significance for the growth, development, and metabolic activities of the human body.

testing:

During the ongoing catalase powder detection, bubbles can be observed.
Catalase detection is one of the three main methods used by microbiologists to identify bacterial species, which involves using hydrogen peroxide to detect the presence of catalase. If bacteria contain catalase, adding a small amount of bacterial extract to the hydrogen peroxide solution can observe the formation of oxygen bubbles.

 

If bubbles are generated, the bacterium is considered to be "catalase positive". Such as Staphylococcus and Micrococcus. If not, the bacterium is considered to be "catalase negative". Such as streptococcus and enterococcus. Although catalase detection cannot identify specific organisms, when combined with other detection methods, it can effectively assist in diagnosis.
In addition, the presence of catalase in bacteria also depends on cell growth conditions and the culture medium used.

 

Distribution:

Catalase is present in various tissues of all known animals, particularly at high concentrations in the liver. In the bomber beetle, catalase has a unique use. This beetle has two sets of chemicals stored separately in its glands. Large glands store hydroquinone and hydrogen peroxide, while small glands store catalase and horseradish peroxidase. When beetles mix chemicals from two glands together, they release oxygen, which can both oxidize hydroquinone and act as a booster.

 

Catalase is also commonly found in plants, but not in fungi, although some fungi have been found to produce the enzyme in low pH and warm environments.
The vast majority of aerobic microorganisms contain catalase. The exception includes Streptococcus, an aerobic bacterium without catalase. Some anaerobic microorganisms, such as Methanosarcina barkeri, also contain catalase.

Function Overview

 

Hydrogen peroxide is a waste generated during metabolic processes that can cause damage to the body. To avoid such damage, hydrogen peroxide must be rapidly converted into other harmless or less toxic substances. And catalase is often used by cells as a tool to catalyze the decomposition of hydrogen peroxide.
But the true biological importance of catalase is not so simple: researchers have found that genetically engineered mice with catalase deficiency still exhibit normal phenotypes, indicating that catalase is only essential for animals under certain specific conditions.

 

Some people have very low levels of catalase powder in their bodies, but they also do not show obvious pathological reactions. This is likely because the main hydrogen peroxide scavenger in normal mammalian cells is peroxiredoxin, not catalase.
Catalase is typically located in an organelle called peroxisomes. Peroxisomes in plant cells participate in photorespiration (utilizing oxygen to generate carbon dioxide) and symbiotic nitrogen fixation (dissociating nitrogen (N2) into active nitrogen atoms).
But when cells are infected by pathogens, hydrogen peroxide can be used as an effective antimicrobial agent. Some pathogens, such as Mycobacterium tuberculosis, Legionella pneumophila, and Campylobacter jejuni, can produce catalase to degrade hydrogen peroxide, allowing them to survive in the host's body.

Bleach effect:

 

It should be noted that enzymes can promote bleaching, and bleaching wool in a hydrogen peroxide bleaching solution containing the protease Bactosol ST can significantly improve the whiteness and hydrophilicity of wool. This is because enzymes promote rapid initial erosion of wool fibers, making wool bleaching easier to carry out. Starting from this principle, pre treating wool with protease to expose the fiber surface before bleaching is obviously more effective, and fiber damage is also easier to control.

 

Touching enzyme

Catalase (CAT) is an enzyme scavenger, also known as a peroxidase, which is a binding enzyme with iron porphyrin as a secondary group. It can promote the decomposition of H2O2 into molecular oxygen and water, eliminate hydrogen peroxide in the body, and thus protect cells from the toxicity of H2O2. It is one of the key enzymes in the biological defense system. The mechanism by which CAT acts on hydrogen peroxide is essentially the dismutation of H2O2, which requires two H2O2 molecules to meet and collide with CAT at the active center in order for the reaction to occur. The higher the concentration of H2O2, the faster the decomposition rate.

This is a stable hydrogen peroxide decomposition enzyme that can decompose hydrogen peroxide into water and oxygen without affecting fibers and dyes. Therefore, after bleaching and before dyeing, residual hydrogen peroxide on bleached fabrics and in dyeing tanks is removed by H2O2 decomposition enzyme to avoid further oxidation of fibers and oxidation of dyes during dyeing. At the same time, it can shorten processing time, reduce water consumption for washing, and decrease the amount of wastewater. Especially suitable for yarns, tube yarns, and knitted fabrics. Similarly, the activity of catalase changes with pH and temperature, with the highest activity occurring around pH 7 and 30-40 ℃. An increase in hydrogen peroxide concentration will accelerate the decomposition reaction rate, but it must be noted that when the concentration exceeds a certain amount, the enzyme's effect will weaken, and excessive residual H2O2 is detrimental to fibers and dyes. So the amount of H2O2 cannot be arbitrarily increased just because of the presence of H2O2 degrading enzyme. When using, it is usually important to pay attention to the compatibility of H2O2 decomposing enzymes with commonly used surfactants and H2O2 stabilizers. In actual production applications, the pH is 6-8, the temperature is 20-55 ℃, the enzyme dosage is 5-10 KCLU/liter, and the time is 10-20 minutes. This technology has gradually been recognized and accepted domestically, and it is very beneficial for improving the brightness of reactive dyes.

Although the complete catalytic mechanism of catalase is not yet fully understood, its catalytic process is believed to be divided into two steps:
H2O2 + Fe(III)-E → H2O + O=Fe(IV)-E(.+)
H2O2 + O=Fe(IV)-E(.+) → H2O + Fe(III)-E + O2
Among them, "Fe() - E" represents the central iron atom (Fe) of the heme group (E) bound to the enzyme. Fe (IV) - E (.+) is a resonant form of Fe (V) - E, in which the iron atom is not completely oxidized to+V valence, but rather receives some "supporting electrons" from the heme. Therefore, the heme in the reaction equation is also represented as a free radical cation (.+)

Hydrogen peroxide enters the active site and interacts with the asparagine residue at position 147 (Asn147) and the histidine residue at position 74 (His74) of the enzyme, causing a proton to transfer between oxygen atoms. Free oxygen atoms coordinate and combine to form water molecules and Fe (IV)=O. Fe (IV)=O reacts with the second hydrogen peroxide molecule to re form Fe (III) - E, generating water molecules and oxygen. The reactivity of the iron atom in the active center may be enhanced by the presence of the phenolic side chain of the tyrosine residue (Tyr357) at position 357, which assists in the oxidation of Fe (III) to Fe (intermediate reaction). The rate of this reaction can usually be determined by the Mie equation.

Catalase powder can also oxidize other cytotoxic substances such as formaldehyde, formic acid, phenol, and ethanol. These oxidation processes require the use of hydrogen peroxide to complete through the following reactions:
H2O2 + H2R → 2H2O + R
Similarly, the specific reaction mechanism is still unclear.
Any heavy metal ion (such as copper ions in copper sulfate) can serve as a non competitive inhibitor of catalase. In addition, highly toxic cyanide is a competitive inhibitor of catalase, which can tightly bind to the heme in the enzyme and prevent its catalytic reaction.
The three-dimensional structure of the peroxidase intermediate in a peroxide state has been resolved and can be retrieved from protein databases.

Hot Tags: catalase powder cas 9001-05-2, suppliers, manufacturers, factory, wholesale, buy, price, bulk, for sale, naphtho 2 1 b benzofuran 4 yl 1 1 2 2 3 3 4 4 4 nonafluorobutane 1 sulfonate, CAS 2644646 42 2, 1H BenziMidazole 1 4 broMophenyl 2 phenyl, N7 dibenzo b d thiophen 3 yl N2 N2 N7 triphenyldibenzo b d thiophene 2 7 diamine, 4 bromo 1 1 4 1 terphenyl, CAS 2457172 98 2