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25810

Sigma-Aldrich

Chloroperoxidase from Caldariomyces fumago

aqueous suspension, brown, >10,000 U/mL

Synonym(s):

Chloride Peroxidase, Chloride:hydrogen-peroxide oxidoreductase

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

fungus (Caldariomyces fumago)

form

aqueous suspension

concentration

>10,000 U/mL

color

brown

storage temp.

2-8°C

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General description

Chloroperoxidase (CPO) is a major heme-containing, synthetic and versatile enzyme, obtained from Caldariomyces fumago.

Application

A useful alternative to lactoperoxidase for 131I ion labeling studies, for bromination of proteins, and for 36Cl labeling of macromolecules in long-term isolation procedures.

Biochem/physiol Actions

Chloroperoxidase (CPO) helps in the catalysis of oxidation reactions with the help of hydrogen peroxide. It displays peroxidase, catalase and cytochrome P450-like functions. CPO also plays a role in catalyzing halogenation reactions.

Unit Definition

1 U corresponds to the amount of enzyme which converts 1 μmol of monochlorodimedone to dichlorodimedone per minute at pH 2.75 and 25 °C in the presence of KCl and H2O2.

Physical form

Supplied as a suspension in 0.1 M sodium phosphate pH 4.0.

Other Notes

Oxidation of aminopyrine; Chloroperoxidase, a peroxidase with potential; Chloroperoxidase-catalyzed asymmetric transformations.

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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H Sayo et al.
Chemical & pharmaceutical bulletin, 37(12), 3347-3350 (1989-12-01)
Although in the absence of halide ion chloroperoxidase did not catalyze the ethylhydroperoxide (EHP)-supported oxidation of aminopyrine, in the presence of Br- or Cl-, chloroperoxidase did catalyze the oxidation of aminopyrine, generating the aminopyrine cation radical (AP+). The initial rate
M.A. Pickard et al.
Journal of Industrial Microbiology, 7, 235-235 (1991)
Fast and efficient purification of chloroperoxidase from C. fumago
Yazbik V and Ansorge SM
Process. Biochem., 45(2), 279-283 (2010)
H. Fu et al.
The Journal of Organic Chemistry, 57, 7265-7265 (1992)
S. Colonna et al.
NATO ASI Ser., Ser. C, 381, 323-323 (1992)

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