Novel high-performance catalase purified from a psychrotolerant bacterial origin, produced recombinantly in non-pathogenic strain of E. coli.
Catalase is an enzyme that catalyzes the transformation of hydrogen peroxide into water and oxygen. This enzyme functions as a natural antioxidant protecting the cell against oxidative damage. This enzyme finds applications in Research and Clinical Chemistry. It also finds diverse industrial applications in textiles, waste treatment, cosmetics and as a disinfectant agent.
Read a related blog post, A novel catalase from an extreme microorganism.
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|Source:||Escherichia coli (recombinant enzyme from psychrotolerant bacterium)|
|Molecular Weight:||~55 kDa subunit. Tetrameric protein|
|Activity:||>8000 U/mg protein. One unit is defined as the decomposition of 1umol of H2O22 in 1 Unit Definition minute at 25C at pH 7.0. The rate of disappearance of H2O2 is observed at 240 nm|
|Temperature Range:||20-80C (optimum: 30-40C)|
|pH Range:||4-9.5 (optimum: 7.5)|
|Storage:||At -20C, it keeps 100% of its activity for more than two years|
Catalase Activity vs. Temperature
Swissaustral Catalase is more stable than catalases from fungal and bovine liver sources in a broad spectrum of temperatures offering close to optimal activity between 20C and 70C
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