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Merck

B0390

Sigma-Aldrich

Bilirubin Oxidase from Myrothecium verrucaria

greener alternative

lyophilized powder, 15-65 units/mg protein

Sinónimos:

MvBOx, Bilirubin:oxygen oxidoreductase

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About This Item

Número de CAS:
Comisión internacional de enzimas:
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

Greener Alternative Product

technique(s)

toxicology assay: suitable

greener alternative category

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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Referencia del producto
Descripción
Precios

Substrate

Referencia del producto
Descripción
Precios

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Emmanuel Suraniti et al.
Analytical chemistry, 83(7), 2824-2828 (2011-03-17)
Immobilization and electrical wiring of enzymes is of particular importance for the elaboration of efficient biosensors and can be cumbersome. Here, we report a fast and easy protocol for enzyme immobilization, and as a proof of concept, we applied it
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
Bilirubin oxidase activity of Bacillus subtilis CotA
Sakasegawa S, et al.
Applied and Environmental Microbiology, 72(1), 972-975 (2006)
Dan Wen et al.
Analytical chemistry, 83(10), 3968-3972 (2011-04-19)
A self-powered electrochemical sensor has been facilely designed for sensitive detection of Hg(2+) based on the inhibition of biocatalysis process of enzymatic biofuel cell (BFC) for the first time. The as-prepared one-compartment BFC, which was consisted of alcohol dehydrogenase supported
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)

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