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CAS NO: 9001-05-2
EC NO: 1.11.1.6
Catalase is a common enzyme found in nearly all living organisms exposed to oxygen (such as bacteria, plants, and animals) which catalyzes the decomposition of hydrogen peroxide to water and oxygen.
Catalase is a very important enzyme in protecting the cell from oxidative damage by reactive oxygen species (ROS). Likewise, catalase has one of the highest turnover numbers of all enzymes; one catalase molecule can convert millions of hydrogen peroxide molecules to water and oxygen each second.
Catalase is a tetramer of four polypeptide chains, each over 500 amino acids long.
Catalase contains four iron-containing heme groups that allow the enzyme to react with hydrogen peroxide. The optimum pH for human catalase is approximately 7,and has a fairly broad maximum: the rate of reaction does not change appreciably between pH 6.8 and 7.5.The pH optimum for other catalases varies between 4 and 11 depending on the species. The optimum temperature also varies by species.
History
Catalase was first noticed in 1818 by Louis Jacques Thénard, who discovered hydrogen peroxide (H2O2). Thénard suggested its breakdown was caused by an unknown substance. In 1900, Oscar Loew was the first to give it the name catalase, and found it in many plants and animals.In 1937 catalase from beef liver was crystallised by James B. Sumner and Alexander Dounce and the molecular weight was found in 1938.
The amino acid sequence of bovine catalase was determined in 1969, and the three-dimensional structure in 1981.
Catalase, an enzyme that brings about (catalyzes) the reaction by which hydrogen peroxide is decomposed to water and oxygen. Found extensively in organisms that live in the presence of oxygen, catalase prevents the accumulation of and protects cellular organelles and tissues from damage by peroxide, which is continuously produced by numerous metabolic reactions. In mammals, catalase is found predominantly in the liver.
Catalase has various industrial applications. In the food industry, it is used in combination with other enzymes in the preservation of foodstuffs and in the manufacture of beverages and certain food items. Commercial catalases also are used to break down hydrogen peroxide in wastewater.
Catalase is an enzyme that catalyzes the decomposition of hydrogen peroxide. The system name of 2H2O2—→2H2O+O2 is H2O2; H2O2 is oxidoreductase (E, C, 1, 11, 1, 6).
Catalases cofactor is heme and molecular weight is 250,000, existing in the form of tetramer.
Catalase is present in almost all animal cells. In addition to the true anaerobes, this enzyme is widely used in plants and in all microbes.
Almost all biological organisms have catalase.
Catalase is common in breathing organisms, mainly in the plants' chloroplasts, mitochondria, endoplasmic reticulum, animal liver and red blood cells.Its enzymatic activity provides antioxidant defense mechanism to the body.
Catalase is a red blood hormone enzyme. Different sources have different structures.The level of activity is different in different tissues.Hydrogen peroxide decomposes faster in the liver than in brain or heart organs, which is due to the high levels of Catalase in the liver.
General-purpose Name: catalase
English name: CATALASE FROM MICROCOCCUS
Aliases: catalase isolated from streptococcus hemolytic streptococcus
Cas No：9001-05-2
Catalase is used in the food industry to remove hydrogen peroxide in milk used to make cheese.
Catalase is also used in food packaging to prevent food from being oxidized. In the textile industry, catalase is used to remove hydrogen peroxide from textiles to ensure that the finished product is free from peroxide.
Catalase is also used in the cleaning of contact lenses: glasses are soaked in cleaning agents containing hydrogen peroxide, and then residual hydrogen peroxide is removed with catalase before use. The use of catalase in the beauty industry: the enzyme and hydrogen peroxide are added to some facial care to increase the amount of oxygen in the upper layer of the epidermis.
Catalase is often used in the laboratory as a tool to understand the effects of enzymes on the rate of reaction.
Uses
In combination with glucose oxidase, for treatment of food wrappers to prevent oxidative deterioration of food: Sarett, Scott, US 2765233 (1956 to Ben L. Sarett). In the removal of traces of peroxide in the process of cold sterilization (preservation of milk and cheese by treatment with hydrogen peroxide). With glucose oxidase, q.v., in food preservation.
Catalase is also ubiquitous in plants and does not include fungi, although some fungi have been found to be able to produce this enzyme in low pH and warm conditions. The vast majority of aerobic microorganisms contain catalase, except for streptococcus, an aerobic bacteria without catalase. Some anaerobic microbes, such as methanosarcina barkeri, also contain catalase.
Catalase is present in all tissues of all known animals, especially in the liver at high concentrations.In the bombardier beetle, catalase has a unique purpose. The beetle has two sets of chemicals stored separately in the gland. The large glands store hydroquinone and hydrogen peroxide. The small glands store catalase and horseradish peroxidase. When the beetle mixes the chemicals in the two glands, it releases oxygen. Oxygen can oxidize hydroquinone can act as a booster.
Catalase has various physiological functions.
Catalase can not only regulate the H2O2 level in the body, but also act as a protective agent for Hb and other sulfhydryl protein. The changes in serum Catalase activity are seen in the following diseases:The increase of Catalase is mainly seen in liver cirrhosis, typhoid, fever etc..
The decrease of Catalase is mainly seen in all kinds of cancer, myocarditis, pneumonia, acute cholecystitis, acute pancreatitis etc..The serum Catalase of starvation, rheumatic fever, trauma, local purulent infection, anemia and so on can also be reduced in varying degrees.
About this substance
Helpful information
Catalase is registered under the REACH Regulation and is manufactured in and / or imported to the European Economic Area, at ≥ 10 to < 100 tonnes per annum.
Catalase is used by consumers, in articles, by professional workers (widespread uses), in formulation or re-packing, at industrial sites and in manufacturing.
Consumer Uses
Catalase is used in the following products: washing & cleaning products.
Other release to the environment of Catalase is likely to occur from: indoor use as processing aid.
Article service life
Other release to the environment of Catalase is likely to occur from: indoor use in long-life materials with low release rate (e.g. flooring, furniture, toys, construction materials, curtains, foot-wear, leather products, paper and cardboard products, electronic equipment). ECHA has no public registered data indicating whether or into which articles the substance might have been processed.
Widespread uses by professional workers
Catalase is used in the following products: laboratory chemicals.
Catalase is used in the following areas: health services.
Other release to the environment of Catalase is likely to occur from: indoor use as processing aid.
Formulation or re-packing
Catalase is used in the following products: laboratory chemicals, washing & cleaning products and water treatment chemicals.
Release to the environment of Catalase can occur from industrial use: formulation of mixtures.
Uses at industrial sites
ECHA has no public registered data indicating whether or in which chemical products the substance might be used.
Catalase is used in the following areas: offshore mining, municipal supply (e.g. electricity, steam, gas, water) and sewage treatment and scientific research and development.
Catalase is used for the manufacture of: pulp, paper and paper products, chemicals and textile, leather or fur.
Release to the environment of Catalase can occur from industrial use: in processing aids at industrial sites and in the production of articles.
Manufacture
Release to the environment of Catalase can occur from industrial use: manufacturing of the substance.
Catalase activates the decomposition of hydrogen peroxide, a reactive oxygen species, into water and oxygen.
Catalase functions as a natural antioxidant, protecting cells against oxidative damage to proteins, lipids and nucleic acids.
Catalase has also been used to study the role reactive oxygen species play in gene expression and apoptosis.
Catalase, Lyophilized, a tetramer of four polypeptide chains, is used in the food industry to remove hydrogen peroxide from milk in order to make cheese.
Chemical Name: Catalase
CAS Number: 9001-05-2
Molecular Formula: C9H10O3
Molecular Weight: 166.174
Catalog: Food additive Enzyme
Catalase is included in the mitochondrial respiration medium MiR06 (MiR06 = MiR05 plus catalase), so as to allow for re-oxygenation of the respiration medium (without lifting the stopper and risking the introduction of air bubbles) by addition of a small volume of a 200 mM stock solution of H2O2.
Catalase is an enzyme responsible for the degradation of hydrogen peroxide.
Catalase is a protective enzyme present in nearly all animal cells.
Specificity:
The reaction of catalase occurs in two steps. A molecule of hydrogen peroxide oxidizes the heme to an oxyferryl species. A porphyrin cation radical is generated when one oxidation equivalent is removed from iron and one from the poryphyrin ring. A second hydrogen peroxide molecule acts as a reducing agent to regenerate the resting state enzyme, producing a molecule of oxygen and water (Switala and Loewen 2002).
Molecular Characteristics:
The gene that encodes catalase, CAT, is located on chromosome 15 in Bos taurus. The gene is conserved in human, chimpanzee, dog, mouse, rat, chicken, zebrafish, fruit fly, mosquito, C. elegans, S. pombe, S. cerevisiae, K. lactis, E. gossypii, N. crassa, A. thaliana, and rice (Gene ID: 531682).
Applications:
Commercially wherever hydrogen peroxide is used as a germicide
Milk preservative with peroxidase
Increases synthesis and stability of diacetyl in cultured milk
Free radical research
Deodorization
Decomposition of residual hydrogen peroxide after bleaching woven and knitted cotton fabrics before drying
Cysteamine determination
Gluconic and glycolic acid production
Cleaning silicon and semiconductor plates
Catalase is a key enzyme in the metabolism of H2O2 and reactive oxygen species (ROS), and its expression and localization is markedly altered in tumors. Free oxygen radical scavenger.
Catalase (EC 1.11.1.6) is an enzyme which is present mainly in the peroxisomes of mammalian cells.
Catalase is a tetrameric enzyme consisting of four identical, tetrahedrally arranged subunits of 60 kDa, each containing in its active center a heme group and NADPH.
Catalase (EC 1.11.1.6) is a heme-containing enzyme ubiquitously present in most aerobic organisms.
Catalase is the most abundant antioxidant enzyme ubiquitously present in the liver, erythrocytes and alveolar epithelial cells.
Inside cells, it kick starts the breakdown of hydrogen peroxide (H2O2) into water and oxygen. One molecule of catalase can breakdown 10 million molecules of hydrogen peroxide in one second.
Catalase is a characteristic enzyme of peroxisomes, of which it is the most abundant protein.
Catalase is widely used as a typical example of a peroxisomal enzyme during biochemistry and molecular biology teaching due to its specific characteristics, including high efficiency, high specificity and stability.
Catalase is produced naturally and used by humans, animals and plants. Inside cells, the antioxidant enzyme kick starts the breakdown of hydrogen peroxide, which can be toxic, into water and oxygen. The enzyme is also commonly used worldwide in food production and as a dietary supplement.
Catalase (EC 1.11.1.6) is an important antioxidant enzyme responsible for the degradation of the reactive oxygen species, hydrogen peroxide.
Catalase is widely expressed in both mammalian and non-mammalian cells containing the cytochrome system. Catalase catalyses the decomposition of hydrogen peroxide into water and oxygen.
Catalase is an enzyme that catalyzes the decomposition of hydrogen peroxide. The system name of 2H2O2—→2H2O+O2 is H2O2; H2O2 is oxidoreductase (E, C, 1, 11, 1, 6). Its cofactor is heme and molecular weight is 250,000, existing in the form of tetramer.
Catalase is a common enzyme, found in nearly all living organisms.
Catalase catalyses hydrogen peroxide into water and oxygen and protects organisms from free radicals
Catalase also has industrial uses to prevent certain contaminants in food and as a disinfectant for contact lenses and a cleansing agent in some other products.
Food industry
Catalase is widely used in the food industry. Catalase removes hydrogen peroxide from milk thus it aids in cheese production. Catalase prevents food from oxidizing, therefore it can be used in food wrapping.
Cleaning agent
Catalase is sometimes used to disinfect contact lenses. Nowadays, catalase is used in the aesthetics industry in several mask treatments because it help increase cellular oxygenation in the upper layers of epidermis.
Catalase is constantly in battle against the effect of free radicals to the body.
Catalase transforms harmful superoxide radicals into hydrogen peroxide which later breaks down into water and oxygen.
The enzyme catalase is known to catalyse the breakdown of hydrogen peroxide into oxygen and water. Hydrogen peroxide metabolism is mainly regulated by this enzyme.
Catalase is a common enzyme found in nearly all living organisms.
Catalase has one of the highest turnovers of all enzymes as it has the capacity to decompose more than one million molecules of hydrogen peroxide, per molecule of enzyme.
Catalase has been used as an important enzyme in many biotechnological areas including bioremediation.
Catalase is a red crystalline enzyme that consists of a protein complex with hematin groups and catalyzes the decomposition of hydrogen peroxide into water and oxygen.
A manganese protein containing Mn(III) in the resting state, which also belongs here, is often called pseudocatalase
The enzymes from some organisms, such as Penicillium simplicissimum, can also act as a peroxidase Catalase (EC 1.11.1.7) for which several organic substances, especially ethanol, can act as a hydrogen donor
Enzymes that exhibit both catalase and peroxidase activity belong under Catalase EC 1.11.1.21
Product Information
CAS number 9001-05-2
Activity ≥4,000 units/mg dry weight
Unit of Definition One unit is defined as the amount of enzyme that will decompose 1.0 µmol H₂O₂ per min at 30°C, pH 7.0.
EC number 1.11.1.6
Form Green lyophilized powder
Hygroscopic Hygroscopic
PI 5.7 - 8.5
Activity: 11000U/mg
Homogeneous in SDS-PAGE
MW~240000 to 250000
Optimum pH = 7.0
Isoelectric Point = 5.4
DESCRIPTION
Catalase is a common enzyme found in nearly all living organisms exposed to oxygen (such as bacteria, plants, and animals).
It catalyzes the decomposition of hydrogen peroxide to water and oxygen.
APPLICATION
Catalase, for biochemistry Cas 9001-05-2 - used by microbiologists to identify species of bacteria. If the bacteria possess catalase (i.e., are catalase-positive), when a small amount of bacterial isolate is added to hydrogen peroxide, bubbles of oxygen are observed.
Derived from the fungus Aspergillus niger, this enzyme is available in powder or liquid form.
The enzyme is used for the removal of hydrogen peroxide in order to prevent oxidation and inhibit the attachement of the substrate to stainless steel processing equipment. This is especially useful for processing of milk, eggs, fish, and soy proteins.
FUNCTIONS
Catalyst, Enzyme
INDUSTRY
Food Chemicals, Nutrition, Industrial
1.Enzyme preparation. Mainly used in the production of cheese, milk and egg products
2.Common Diagnostic Enzymes
3.Used in biochemical research, food preservation, milk sterilization and de-sugar, etc
As a natural antioxidant, it can be used to study the effect of reactive oxygen species on gene expression and apoptosis
Appearance: White to slight yellow liquid
Catalase is a concentrated industrial grade liquid catalase derived from a submerged fermentation of a genetically modified strain of Bacillus Subtilis.
Catalase is intended for pre-dilution before using.
Catalase is effective for the decomposition of residual hydrogen peroxide after the bleaching of cotton knits and cotton yarn.
Features and Benefits
* Low water consumption
* Short process time
* Safe dyeing
* An environmentally sustainable process
Catalase is a hemoprotein containing four subunits which decomposes peroxide. Catalytic activity is present in nearly all animal cells and organs and in aerobic microorganisms.
Catazyme is produced by fermentation of a selected microorganism followed by purification and formulation. The enzyme effectively catalyzes the hydrolysis of hydrogen peroxide into oxygen and water, which can be widely used in food, textile, paper, electronics, and other industries to remove hydrogen peroxide with a significant saving of water resources and energy.
Catalase is a tetrameric haemin-enzyme, which contains four ferriprotoporphyrin groups per molecule. Chelating agents may remove the iron atom from the haem group of catalase and thereby inactivate it, Bleach formulations usua1ly contain sequestering agents, such as silicates, phosphates or oxalates.
Functions
1. Textile Industry: to remove hydrogen peroxide after bleaching and before dyeing, saving water, energy and time, not damaging the fibers and dyes, and do not pollute the environment;
2. Papermaking Industry: monitoring and optimizing the amount of hydrogen peroxide in bleaching process, degrading residual hydrogen peroxide after the bleaching;
3. Electronics Industry: to remove hydrogen peroxide after eroding germanium, silicon transistors and semiconductor components; saving water, energy and time;
4. Water Treatment: After the use of peroxide for waste water treatment, add catalase to remove the over use of peroxide in case it results in water eutrophication. Also it would not affect other elements in the process because of the specificity of catalase.
IUPAC names
Catalase
catalase
Catalase
Catalase, Aspergillus sp
CatalaseIUBMB 1.11.1.6
hydrogen-peroxide:hydrogen-peroxide oxidoreductase
SYNONYMS:
equilase
Catalase-Agarose
H2O2 oxidoreductase
Catalase from A. niger, lyophil.
Catalase from bovine liver, lyophil.
Catalase-peroxidase
CATALASE FROM BOVINE LIVERCA.65000 U/MG PROTEIN SUSPENSION
CATALASE FROM ASPERGILLUSNIGER CA.2000 U/MG LYOPH.SALT-FREE
CATALASE FROM BOVINE LIVERCA. 11000 U/MG LYOPH. SALTFREE
Catalase from bovine liver,H2O2:H2O2 oxidoreductase
Catalase from Aspergillus niger,H2O2:H2O2 oxidoreductase
Catalase from human erythrocytes,H2O2:H2O2 oxidoreductase
Catalase from murine liver,H2O2:H2O2 oxidoreductase
Catalase from bison liver,H2O2:H2O2 oxidoreductase
Catalase [from Aspergillus niger, 2000 units/mg protein]
Catalase froM bovine liver ca. 11 000 U/Mg lyophil. salt-free
Catalase froM Aspergillus niger ca. 1800 U/Mg lyophil. salt-free
CATALASE FROM BOVINE LIVER, ~1300 U/MG*
CATALASE FROM MICROCOCCUS LYSODEIKTICUS, ~170000 U/ML
CatalasePowder
Catalase/CH8530
catalase from murine liver
CATALASE FROM ASPERGILLUS NIGER GRADE I
Catalase from canine liver
CATALASE FROM MICROCOCCUS LYSODEIKTICU
Catalase, from bovine liver, 2000-5000 units/mg
Catalase, liquid (food grade)
Catalase, Suspension
Catalase, Filtered
Fungalcatalase
optidase
