B0390
Bilirubin Oxidase from Myrothecium verrucaria
lyophilized powder, 15-65 units/mg protein
Synonym(s):
MvBOx, Bilirubin:oxygen oxidoreductase
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
biological source
fungus (Myrothecium verrucaria)
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.
sustainability
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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
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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Product No.
Description
Pricing
substrate
Signal Word
Danger
Hazard Statements
Precautionary Statements
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
Certificates of Analysis (COA)
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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
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)
S S Wong et al.
Annals of clinical and laboratory science, 25(3), 247-251 (1995-05-01)
Owing to the overlapping absorption bands of hemoglobin and bilirubin, spectrophotometric determination of plasma free hemoglobin has been plagued by the interference of bilirubin when the latter is present in significant concentrations. To resolve this problem, bilirubin oxidase from Myrothecium
Akio Ueda et al.
Journal of the American Chemical Society, 133(13), 4840-4846 (2011-03-10)
We have developed a new carbon film electrode material with thornlike surface nanostructures to realize efficient direct electron transfer (DET) with enzymes, which is very important for various enzyme biosensors and for anodes or cathodes used in biofuel cells. The
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
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