Application

Catalase from bovine liver has been used as a component of gloxy, which is one of the most popular oxygen-scavenging systems.

Catalase acts as a natural antioxidant to study the roles of reactive oxygen species in gene expression and apoptosis. It has also been used to protect against oxidative damage to proteins, lipids, and nucleic acids. Industrially, catalses have been used to remove hydrogen peroxide added to milk and cheese, in textile bleaching, and to examine its positive effects on the viability of DNA-repair mutants of E. coli.

Biochem/physiol Actions

Catalase catalyzes the degradation of hydrogen peroxide into water and oxygen. It can also react with alkylhydrogen peroxides, such as methylperoxide and ethylperoxide and the second H₂O₂ molecule can be replaced by methanol, ethanol, propanol, formate and nitrate as a hydrogen donor.

Catalase has an ability to convert solar radiation into reactive oxidant species (ROS). It is involved in regulation of tissue peroxide levels. Mutation in catalase gene result in the progress of essential hypertension (EH).

Components

Catalase from bovine liver is a tetramer consisting of 4 equal subunits each with a 60 kDa molecular weight. Each of these subunits contains iron bound to a protoheme IX group. The enzyme will also strongly bind to NADP, where NADP and the heme group are within 13.7 angstroms.

General description

Catalase is encoded by the gene mapped to human chromosome 11p13. Mammalian catalase is an antioxidant enzyme and is a member of hydroperoxidase family). The active enzyme is homotetrameric in nature.

Packaging

100, 500 mg in poly bottle

1 g in poly bottle

Physical form

Supplied as a lyophilized powder containing ≤0.2% thymol

Unit Definition

One unit will decompose 1.0 micromole of hydrogen peroxide per minute at pH 7.0 at 25 deg C, while the hydrogen peroxide concentration falls from 10.3 to 9.2 millimolar.