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Sigma-Aldrich

Bilirubin Oxidase from Myrothecium verrucaria

greener alternative

lyophilized powder, 15-65 units/mg protein

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Synonym(s):
MvBOx, Bilirubin:oxygen oxidoreductase
CAS Number:
80619-01-8
Enzyme Commission number:
1.3.3.5 (BRENDA, IUBMB)
MDL number:
MFCD00130650
NACRES:
NA.54

biological source

fungus (Myrothecium verrucaria)

Quality Level

200

form

lyophilized powder

specific activity

15-65 units/mg protein

composition

Protein, ≥15% biuret

storage condition

(Keep container tightly closed in a dry and well-ventilated place.)

greener alternative product characteristics

Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.

technique(s)

toxicology assay: suitable

greener alternative category

, Enabling

shipped in

dry ice

storage temp.

−20°C

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General description

We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for energy efficiency and waste prevention when used in biofuel cell research. For more information see the article in biofiles.

Bilirubin oxidase (BOD) belongs to the subclass of the multicopper oxidase family. It is usually found in fungi.Bilirubin Oxidase is composed of three cupredoxin-like domains that result in two active sites formed by four copper ions. Research area: Apoptosis

Application

Bilirubin Oxidase from Myrothecium verrucaria has been used to eliminate the interference of bilirubin. It has also been used to chemically modify with fluorescein derivative (FS) and combined with multivariate calibration to analyse direct bilirubin (dBR) and total bilirubin (tBR).
Bilirubin oxidase is used to degrade bilirubin. Bilirubin oxidase, from Myrothecium verrucaria, may be used to determine free hemoglobin in icteric specimens . It also has potential application in dye effluent decolorization and is a potential treatment for neonatal jaundice.

Biochem/physiol Actions

Bilirubin oxidase (BOD) is a multicopper oxidase that catalyzes the oxidation of bilirubin to biliverdin. Oxygen is the electron acceptor and is reduced to water. The enzyme is used for diagnostic analysis of bilirubin in serum during medical examinations of the serum. It has also been used as an enzymatic catalyst for the cathode of biofuel cells that work under neutral conditions. It is a monomeric protein with a molecular mass of 60 kDa and high reactivity at neutral pH. BOD participates in porphyrin and chlorophyll metabolism.
Bilirubin oxidase (BOD) is capable of oxidizing laccase substrates.

Unit Definition

One unit will oxidize 1.0 μmole of bilirubin per min at pH 8.4 at 37 °C.

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substrate

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Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

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Adenosine, inosine, and hypoxanthine/xanthine measured in tissue and plasma by a luminescence method.
Jabs CM, et al.
Clinical Chemistry, 36(1), 81-87 (1990)
Masayo Iwaki et al.
FEBS letters, 584(18), 4027-4031 (2010-08-24)
Redox-induced protonation state changes of the Glu residue in the multicopper oxidases, CueO and bilirubin oxidase (BO), were studied by attenuated total reflectance-Fourier transform infrared spectroscopy. By monitoring IR bands of the carboxylic acid C=O stretch in the wild-type and
Bilirubin oxidase activity of Bacillus subtilis CotA
Sakasegawa S, et al.
Applied and Environmental Microbiology, 72(1), 972-975 (2006)
James A Cracknell et al.
Dalton transactions (Cambridge, England : 2003), 40(25), 6668-6675 (2011-05-06)
The blue multi-copper oxidase bilirubin oxidase (BOx) from the ascomycete plant pathogen Myrothecium verrucaria (Mv) efficiently catalyses the oxidation of bilirubin to biliverdin, with the concomitant reduction of O(2) to water, a reaction of considerable interest for low-temperature bio-fuel cell
Tomáš Kovaľ et al.
Scientific reports, 9(1), 13700-13700 (2019-09-25)
Unlike any protein studied so far, the active site of bilirubin oxidase from Myrothecium verrucaria contains a unique type of covalent link between tryptophan and histidine side chains. The role of this post-translational modification in substrate binding and oxidation is
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