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Hydrogen peroxide. Catalase is used in the food industry for removing hydrogen peroxide from milk prior to cheese production. [43] Another use is in food wrappers, where it prevents food from oxidizing. [44] Catalase is also used in the textile industry, removing hydrogen peroxide from fabrics to make sure the material is peroxide-free. [45]
In enzymology, a NADH peroxidase (EC 1.11.1.1) is an enzyme that catalyzes the chemical reaction. NADH + H + + H 2 O 2 NAD + + 2 H 2 O. The presumed function of NADH peroxidase is to inactivate H 2 O 2 generated within the cell, for example by glycerol-3-phosphate oxidase during glycerol metabolism or dismutation of superoxide, before the H 2 O 2 causes damage to essential cellular components.
d -Glucose + 2 [NAD] + + 2 [ADP] + 2 [P] i 2 × Pyruvate 2 × + 2 [NADH] + 2 H + + 2 [ATP] + 2 H 2 O Glycolysis pathway overview The use of symbols in this equation makes it appear unbalanced with respect to oxygen atoms, hydrogen atoms, and charges. Atom balance is maintained by the two phosphate (P i) groups: Each exists in the form of a hydrogen phosphate anion, dissociating to contribute ...
Class I, the intracellular peroxidases, includes: cytochrome c peroxidase (CCP), a soluble protein found in the mitochondrial electron transport chain, where it probably protects against toxic peroxides; ascorbate peroxidase (AP), the main enzyme responsible for hydrogen peroxide removal in chloroplasts and cytosol of higher plants; [4] and ...
Hydrogen peroxide is a chemical compound with the formula H 2 O 2.In its pure form, it is a very pale blue [5] liquid that is slightly more viscous than water.It is used as an oxidizer, bleaching agent, and antiseptic, usually as a dilute solution (3%–6% by weight) in water for consumer use and in higher concentrations for industrial use.
Glutathione peroxidases use glutathione as an electron donor and are active with both hydrogen peroxide and organic hydroperoxide substrates. Gpx1, Gpx2, Gpx3, and Gpx4 have been shown to be selenium-containing enzymes, whereas Gpx6 is a selenoprotein in humans with cysteine-containing homologues in rodents.
The 3 substrates of this enzyme are Mn(II), H +, and H 2 O 2, whereas its two products are Mn(III) and H 2 O. This enzyme belongs to the family of oxidoreductases, to be specific those acting on a peroxide as acceptor (peroxidases). The systematic name of this enzyme class is Mn(II):hydrogen-peroxide oxidoreductase.
Horseradish peroxidase is also commonly used in techniques such as ELISA and Immunohistochemistry due to its monomeric nature and the ease with which it produces coloured products. Peroxidase, a heme-containing oxidoreductase, is a commercially important enzyme which catalyses the reductive cleavage of hydrogen peroxide by an electron donor.
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