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C3515

Sigma-Aldrich

Catalase from Aspergillus niger

ammonium sulfate suspension, ≥4,000 units/mg protein

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Synonym(s):
H2O2:H2O2 oxidoreductase
CAS Number:
Enzyme Commission number:
MDL number:
eCl@ss:
32160410
NACRES:
NA.54

biological source

Aspergillus niger

form

ammonium sulfate suspension

specific activity

≥4,000 units/mg protein

mol wt

tetramer ~250 kDa

storage condition

(Tightly closed)

technique(s)

FISH: suitable

UniProt accession no.

shipped in

wet ice

storage temp.

2-8°C

InChI

1S/C9H10O3/c1-2-12-9(11)7-3-5-8(10)6-4-7/h3-6,10H,2H2,1H3

InChI key

NUVBSKCKDOMJSU-UHFFFAOYSA-N

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C3556C100C40
vibrant-m

C3515

Catalase from Aspergillus niger

vibrant-m

C3556

Catalase from human erythrocytes

vibrant-m

C100

Catalase from bovine liver

vibrant-m

C40

Catalase from bovine liver

biological source

Aspergillus niger

biological source

human erythrocytes

biological source

-

biological source

-

specific activity

≥4,000 units/mg protein

specific activity

≥30,000 units/mg protein

specific activity

40,000-60,000 units/mg protein (E1%/405)

specific activity

≥10,000 units/mg protein

mol wt

tetramer ~250 kDa

mol wt

tetramer ~250 kDa

mol wt

tetramer ~250 kDa

mol wt

tetramer ~250 kDa

storage condition

(Tightly closed)

storage condition

(Tightly closed. Dry. Keep locked up or in an area accessible only to qualified or authorized
persons)

storage condition

-

storage condition

-

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

−20°C

General description

Research area: Cell Signaling

Catalase is an active enzyme present in aerobic organisms. It is a ferric hemoprotein and a tetramer.

Application

Catalase from Aspergillus niger has been used:
  • as a positive control during the functional characterization of Clostridium difficile spore coat proteins.
  • as a component of the catalase solution to prepare GLOX buffer with enzymes to maintain the embryos of Caenorhabditis elegans before single-molecule fluorescence in situ hybridization (smFISH) studies
  • as a component of the imaging buffer for stochastic optical reconstruction microscopy (STORM) imaging of platelet-rich plasma
  • as a supplement in Todd Hewitt media plus 0.5 % yeast extract (THY) media for the neutralization of pneumococcal H2O2

Biochem/physiol Actions

Catalase catalyzes the decomposition of hydrogen peroxide into water and oxygen. Each subunit of the tetramer contains iron bound to a protoheme IX group. The enzyme also strongly binds NADP, which is in close proximity to the heme group. Isoelectric point is found to be 6.5. Optimum pH for catalytic activity is 7.0. The enzyme activity is inhibited by 3-amino-1-H-1,2,4 triazole, cyanide, azide, hydroxylamine, cyanogen bromide, 2-mercaptoethanol, dithiothreitol, dianisidine, and nitrate. Incubation of catalase with ascorbate or ascorbate/Cu2+ results in degradation of the catalase molecule.
Catalase is involved in catalyzing the degradation of hydrogen peroxide (H2O2) to water and free oxygen. Catalase is used commercially for decomposing H2O2 as it is added as an antimicrobial agent in process streams. It also catalyzes the oxidation of electron donors like ethanol and phenols during lower concentrations of H2O2. Catalase shows antioxidant activity by protecting cells from higher levels of reactive oxygen species (ROS). Increased expression of catalase is observed in chronic lymphocytic leukemia, gastric cancer, glioma, and melanoma. Decreased levels of catalase are seen in acute myeloid leukemia, lung, pancreatic, prostate, and skin (non-melanoma) cancers. Hence catalase exhibits a dual role in cancer.

Caution

Freezing of solutions is not recommended.

Unit Definition

One unit will decompose 1.0 μmole of H2O2 per min at pH 7.0 at 25 °C, while the H2O2 concentration falls from 10.3 to 9.2 mM, measured by the rate of decrease of A240.

Physical form

Suspension in 3.2 M (NH4)2SO4 solution, pH 6.0

Analysis Note

Protein determined by biuret

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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J Fiedurek et al.
Journal of applied microbiology, 89(1), 85-89 (2000-08-17)
A novel method for increasing dissolved oxygen concentration in culture media has been developed. It involves adding hydrogen peroxide (H2O2) to the medium which is then decomposed to oxygen and water by catalase. Some factors affecting oxygenation of culture were
3D structure modeling of catalase enzyme from Aspergillus Fumigatus
Dwivedi V D, et al.
Open journal of immunology, 1(1) (2016)
Seleipiri Charles et al.
Analytical chemistry, 93(3), 1369-1376 (2020-12-24)
Recent development in fluorescence-based molecular tools has contributed significantly to developmental studies, including embryogenesis. Many of these tools rely on multiple steps of sample manipulation, so obtaining large sample sizes presents a major challenge as it can be labor-intensive and
L Brunelli et al.
Free radical biology & medicine, 30(7), 709-714 (2001-03-29)
Previously, we found that catalase enhanced the protection afforded by superoxide dismutase to Escherichia coli against the simultaneous generation of superoxide and nitric oxide (Brunelli et al., Arch. Biochem. Biophys. 316:327-334, 1995). Hydrogen peroxide itself was not toxic in this
M E Percy
Canadian journal of biochemistry and cell biology = Revue canadienne de biochimie et biologie cellulaire, 62(10), 1006-1014 (1984-10-01)
Although animal catalase has been studied for decades, its physiological role has remained perplexing. It has two enzymatic functions, not only catalyzing the breakdown of H2O2 into O2 and H2O, but also in the presence of low concentrations of H2O2

Articles

Instructions for working with enzymes supplied as ammonium sulfate suspensions

Protocols

This procedure may be used for all Catalase products.

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