Literature DB >> 22862914

Purification, characterization and decolorization of bilirubin oxidase from Myrothecium verrucaria 3.2190.

Xu Han1, Min Zhao, Lei Lu, Yanhong Liu.   

Abstract

Myrothecium verrucaria 3.2190 is a nonligninolytic fungus that produces bilirubin oxidase. Both M. verrucaria and the extracellular bilirubin oxidase were tested for their ability to decolorize indigo carmine. The biosorption and biodegradation of the dye were detected during the process of decolorization; more than 98% decolorization efficiency was achieved after 7 days at 26°C. Additionally, the crude bilirubin oxidase can efficiently decolorize indigo carmine at 30°C~50°C, pH 5.5~9.5 with dye concentrations of 50 mg l(-1)~200 mg l(-1). Bilirubin oxidase was purified and visualized as a single band on native polyacrylamide gel electrophoresis (PAGE). Several enzymatic properties of the purified enzyme were investigated. Moreover, the identity of the purified bilirubin oxidase (BOD) was confirmed by matrix assisted laser desorption ionisation time-of-flight mass spectrometry (MALDI-TOF-MS). These results demonstrate that the purified bilirubin oxidase in M. verrucaria strain has potential application in dye effluent decolorization.
Copyright © 2012 The British Mycological Society. All rights reserved.

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Year:  2012        PMID: 22862914     DOI: 10.1016/j.funbio.2012.05.003

Source DB:  PubMed          Journal:  Fungal Biol


  1 in total

1.  Trp-His covalent adduct in bilirubin oxidase is crucial for effective bilirubin binding but has a minor role in electron transfer.

Authors:  Tomáš Kovaľ; Leona Švecová; Lars H Østergaard; Tereza Skalova; Jarmila Dušková; Jindřich Hašek; Petr Kolenko; Karla Fejfarová; Jan Stránský; Mária Trundová; Jan Dohnálek
Journal:  Sci Rep       Date:  2019-09-23       Impact factor: 4.379

  1 in total

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