Merck, B0390-25UN, Bilirubin Oxidase from Myrothecium verrucaria

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