Catalase-peroxidase
Catalase From Micrococcus Lysodeikticus
CAS: 9001-05-2
Molecular Formula: C9H10O3
Catalase-peroxidase - Names and Identifiers
Catalase-peroxidase - Physico-chemical Properties
| Molecular Formula | C9H10O3 |
| Molar Mass | 166.1739 |
| Density | 1.06g/mLat 20°C |
| Flash Point | 41°C |
| Water Solubility | 125g/L at 25℃ |
| Solubility | Soluble in water and dilute buffer, insoluble in organic solvents. Soluble with warm water. |
| Vapor Presure | 0Pa at 25℃ |
| Appearance | suspension |
| Color | deep brown |
| Merck | 13,1910 |
| Storage Condition | -20°C |
| Stability | Air and moisture sensitive. Incompatible with strong oxidizing agents. Refrigerate. |
| Sensitive | Hygroscopic |
| MDL | MFCD00081483 |
| Physical and Chemical Properties | An amorphous powder or liquid nearly white to light brownish yellow. The molecular weight is about 240,000. Soluble in water, the aqueous solution is generally light brown yellow to brown, almost insoluble in ethanol, chloroform and ether. The optimum pH value is 7.0, which is blocked in dilute acid. The optimum temperature is 0~10 ℃, the temperature is too high or the concentration of hydrogen peroxide can destroy its activity. 1 molecule of catalase can destroy about 5 million hydrogen peroxide molecules within 1min. The main principle of action is: the optimum pH value of the liver is about 7.0, the activity is very high between 5.3 and 8.0, and it decreases quickly below 5.0. The pH value of the aspergillus nigricans is very active between 2 and 7, and the optimum pH value of the small cocci is 7 to 9. Natural products exist in aerobic microorganisms, mammalian red blood cells, liver (extremely rich), etc. |
| Use | Can be used for food preservation, milk sterilization and sugar removal |
Catalase-peroxidase - Risk and Safety
| Risk Codes | 10 - Flammable |
| Safety Description | S23 - Do not breathe vapour. S24/25 - Avoid contact with skin and eyes. S22 - Do not breathe dust. |
| UN IDs | UN 1993 3/PG 3 |
| WGK Germany | 1 |
| RTECS | FI4378000 |
| FLUKA BRAND F CODES | 10-21 |
| TSCA | Yes |
| HS Code | 35079090 |
Catalase-peroxidase - Nature
Open Data Verified Data
general goods have crystals, aqueous suspension (4 ℃ stable), glycerol ethanol solution (4 ℃ after a few months can have a slight turbidity), freeze-dried products (4 ℃, after six months, no decrease in viability) and dry powder. The range of activity was pH4 ~ 9, the optimum pH was 6.8, and the optimum temperature was 40. Crystal Water suspension containing 0. 5% thymol and 30% glycerol, 0~4 ℃ can be stable for more than one year.
Last Update：2024-01-02 23:10:35
Catalase-peroxidase - Use
Open Data Verified Data
commonly used diagnostic enzymes. With the coupling reaction, determination of glucose and so on. Food preservation, decomposition of hydrogen peroxide. Biochemical reagents.
Last Update：2022-01-01 11:16:50
Catalase-peroxidase - Safety
Open Data Verified Data
1g/bottle, sealed and stored at 0 °c.
Last Update：2022-01-01 11:16:50
Catalase-peroxidase - Vitality definition
1u refers to the decomposition of 7.0 mu mole of H2O2 per minute at pH 1.0, 25 deg C conditions, while the concentration of H2O2 will be reduced from 10.3 to 9.2 mM
Last Update：2023-08-16 21:32:38
Catalase-peroxidase - Stability
The temperature is controlled at 40~45 °c, 55 °c or more, and the drying is stable at room temperature. Ca2 has a protective and activating effect on it.
Last Update：2023-08-16 21:32:38
Catalase-peroxidase - PH
5.0～8.0
Last Update：2023-08-16 21:32:38
Catalase-peroxidase - Reference Information
| LogP | -1.3 at 20℃ |
| EPA chemical substance information | information provided by: ofmpeb.epa.gov (external link) |
| Background and overview | catalase is an enzyme that catalyzes the breakdown of hydrogen peroxide molecules. 2H2O2-→ 2H2O O2 system named H2O2; H2O2 oxidoreductase (E, C, 1, 11, 1, 6), its prosthetic group is heme, molecular weight of 250,000, present as a tetramer. Catalase is present in almost all animal cells and is widely present in plants and in all microorganisms except true anaerobes. Animal liver, red blood cells, kidney contains a particularly rich catalase, mainly in the cells of the micro body (also known as peroxidase body). in the mitochondrial respiratory chain, the electron transfer in the flavinase reaction and other oxidation reactions, some toxic redox reaction products will or may be generated, the most important is the superoxide ion O2-and H2O2, they are very active in chemical properties, may irreversibly damage some biological molecules, into hydrogen peroxide and oxygen. The most important role of peroxyperoxide enzyme is to decompose hydrogen peroxide, prevent the accumulation of hydrogen peroxide, and protect the cells from hydrogen peroxide. Catalase catalyzes the decomposition of hydrogen peroxide very quickly, 104 times faster than peroxidase, each molecule of enzyme catalyzes the decomposition of 44000 molecules of hydrogen peroxide per second. due to the distribution of various types of natural extreme environment in China, it has rich resources of extreme microorganisms, and has increased efforts to develop catalase of all kinds of extreme microorganisms, and continuously improve the level of enzyme production, it is expected to change the situation of China's dependence on the import of catalase. with the continuous development of modern biotechnology and bioinformatics, it will be possible to modify and modify extreme enzymes in vitro, the development and application of CAT produced by extreme microorganisms will show more attractive prospects. |
| medicinal product overview | Common name: CATALASE : catalase isolated from hemolytic Streptococcus Cas No:9001-05-2 structural formula: |
| Clinical significance | CAT has a variety of physiological functions, which can regulate the level of H2O2 in the body, in turn, it can act as a protective agent for Hb and other thiol-containing proteins. Changes in serum CAT activity can be seen in the following diseases: increased CAT was mainly found in liver cirrhosis, typhoid fever, Fever, etc. decreased CAT was mainly found in various types of cancer, myocarditis, Pneumonia, acute cholecystitis, acute pancreatitis, etc. Hunger, rheumatic fever, trauma, local suppurative infection, anemia and other serum CAT can also be reduced to varying degrees. |
| Source | almost all living organisms have catalase. It is commonly found in respiratory organisms, mainly in plant chloroplasts, mitochondria, endoplasmic reticulum, animal liver and red blood cells. Its enzymatic activity provides antioxidant defense mechanism for the body. CAT is a red blood enzyme, different sources have different structures. The level of activity varies in different tissues. Hydrogen peroxide decomposes faster in the liver than in organs such as the brain or heart because of the high levels of CAT in the liver. |
| reaction mechanism | Although the complete catalytic mechanism of catalase is not fully understood, but its catalytic process is considered to be divided into two steps: where, "Fe()-E" represents the central iron atom (Fe) of the heme group (E) bound to the enzyme. Fe(IV)-E(.) it is a resonant form of Fe(V)-E, that is, the iron atom is not completely oxidized to the V Valence, but receives some "supporting electrons" from the heme ". Therefore, the heme in the reaction formula is also expressed as a radical cation (.) no. 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, A proton is allowed to transfer between oxygen atoms. The free oxygen atoms coordinate to form a water molecule and Fe(IV)= O. Fe(IV)= O reacts with a second hydrogen peroxide molecule to reconstitute Fe(III)-E and to generate water molecules and oxygen. [12] The reactivity of the active center iron atom may be due to the presence of the phenyl side chain of the tyrosine residue at position 357 (Tyr357) (helping the oxidation of Fe(III) to Fe(IV)) and improved. The efficiency of the reaction may be enhanced by the interaction of His74 and Asn147 with reaction intermediates. [12] The rate of this reaction can generally be determined by the Michaelis equation. catalase can also oxidize other cytotoxic substances such as formaldehyde, formic acid, phenol and ethanol. These oxidation processes require the use of hydrogen peroxide through the following reactions: Similarly, the specific mechanism of the reaction is unclear. any heavy metal ion (such as copper ion in copper sulfate) can be used as a non-competitive inhibitor of catalase. In addition, the highly toxic cyanide is a competitive inhibitor of catalase, which can bind tightly to the heme in the enzyme and prevent the catalytic reaction of the enzyme. The Three-dimensional structure of catalase intermediates in the peroxidized state has been resolved and can be retrieved in protein databases. |
| detection | in the ongoing catalase detection, bubbles were observed. catalase detection is one of the three main methods for microbiologists to identify bacterial species, that is, hydrogen peroxide is used to detect the presence of catalase. If the bacteria contain catalase, oxygen bubble formation can be observed by adding a small amount of bacterial extract to the hydrogen peroxide solution. if there is bubble formation, the bacterium is considered to be "catalase positive". Such as Staphyloccus and micrococcus. No, the bacterium is considered "catalase negative". For example, strepdoccus and enteroccus. While the catalase test does not identify a particular organism, it can be effective in aiding diagnosis when combined with other tests. The presence or absence of catalase in bacteria also depends on the cell growth conditions and the medium used. |
| Application | 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 oxidation of food. In the textile industry, catalase is used to remove hydrogen peroxide from textiles to ensure that the finished product is peroxide-free. It is also used in the cleaning of contact lenses: the lenses are soaked in a cleaning agent containing hydrogen peroxide, and the residual hydrogen peroxide is removed by catalase before use. The use of catalase in the beauty industry: some facial treatments have added this enzyme and hydrogen peroxide in order to increase the amount of oxygen in the cells in the upper layers of the epidermis. catalase is also often used in the laboratory as a tool to understand the effect of enzymes on reaction rates. |
| Functional Overview | hydrogen peroxide is a metabolic waste product that can cause damage to the body. In order to avoid such damage, hydrogen peroxide must be rapidly converted to other harmless or less toxic substances. Catalase is a tool that is often used by cells to catalyze the decomposition of hydrogen peroxide. but the true biological importance of catalase is not so simple: the researchers found that the genetically engineered catalase-deficient mice still had a normal phenotype, this indicates that catalase is essential to animals only under certain conditions. The level of catalase in some people is very low, but it does not show obvious pathological reaction. This is most likely because the primary hydrogen peroxide scavenger in normal mammalian cells is peroxide reductase, not catalase. catalase is typically localized in an organelle called a peroxisome. Peroxisomes in plant cells are involved in photorespiration (the use of oxygen and the production of carbon dioxide) and the fixation of symbiotic nitrogen (dissociation of nitrogen (N2) into active nitrogen atoms). However, hydrogen peroxide can be used as an effective antimicrobial agent when cells are infected by pathogens. Some pathogens, such as Mycobacterium tuberculosis, Legionella pneumophila, and Campylobacter jejuni, are capable of producing catalase to degrade hydrogen peroxide, allowing them to survive in the host. bleaching it should be noted that the use of enzymes to promote bleaching, bleaching of wool in hydrogen peroxide bleaching solution containing the protease Bactosol ST, the whiteness and hydrophilicity of wool can be significantly improved. This is because the enzyme promotes the initial rapid erosion of the wool fibers, resulting in easier bleaching of the wool. From this principle, the first pretreatment of the wool protease, so that the fiber surface exposed, and then bleaching, obviously better effect, and fiber damage is easy to control. |
| distribution | catalase is present in various tissues of all known animals, particularly in high concentrations in the liver. In the projectile beetle, catalase has a unique use. The beetle has two separate sets of chemicals stored in the gland. Large glands store hydroquinone and hydrogen peroxide, while small glands store catalase and horseradish peroxidase. When the beetle mixes the chemicals in the two glands, it releases oxygen, which oxidizes hydroquinone and acts as a booster. catalase is also commonly found in plants, but does not include fungi, although some fungi have been found to produce this enzyme at low pH and in warm environments. The vast majority of aerobic microorganisms contain catalase [4]. Exceptions include Streptococcus, an aerobic bacterium without catalase. Some anaerobic microorganisms, such as methanosaccina barkeri, also contain catalase. |
| toxicity | FAO/WHO 2001regulations for those prepared by bovine liver, ADI does not make any restrictions; for those prepared by Micrococcus fibrinolytica and Aspergillus niger, ADI delayed the decision; For those prepared by Penicillium, no provision was made; For those prepared by Trichoderma lysii (Trichoderma reesei), no special provision was made. |
| Use limit | is moderately limited (FDA,§ 173.135,2000). |
| Main reference materials | [1] Chemical space-physicochemical properties of catalase [2] Yulin Yang, he Zhian, chief editor. Laboratory diagnosis of clinical liver disease. Beijing: Chinese Medicine Press. 2007.8 |
| Use | enzyme preparation. It is mainly used in the production of cheese, milk and egg products, etc., to eliminate the specific odor caused by the generation of hydrogen peroxide when irradiated by ultraviolet rays; It can also be used as a baking agent in the manufacture of bread. The highest dose in milk was 20mg/kg. commonly used diagnostic enzymes. With the coupling reaction, determination of glucose and so on. Food preservation, decomposition of hydrogen peroxide. Biochemical reagents. used in biochemical research, food preservation, milk sterilization and sugar removal. It is commonly used as a diagnostic enzyme in clinical practice to measure glucose content. an oxidoreductase that oxidizes hydrogen peroxide to oxygen while reducing another molecule of hydrogen peroxide to water. As a natural antioxidant, it can be used to study the effect of reactive oxygen species on gene expression and apoptosis. It is also used to protect proteins, lipids and nucleic acids from oxidative damage. |
| production method | using bovine liver as raw material, homogenate in 35% dioxane, filter and precipitate with dioxane, the product was crystallized from saturated ammonium sulfate. obtained by purification of bovine liver extract. A. niger var. Was cultured under controlled conditions such as aeration and stirring. extracted and refined from the submerged fermentation broth of micrococus lysodeikticus. |
| category | toxic substances |
| flammability hazard characteristics | thermal decomposition of spicy and irritating smoke |
| storage and transportation characteristics | low temperature ventilation and drying |
| fire extinguishing agent | water, carbon dioxide, foam, dry powder |
Last Update：2024-04-09 19:05:15
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