Title: Purification, characterization and decolorization of bilirubin oxidase from Myrothecium verrucaria 3.2190 Authors
|Han, Xu -|
|Zhao, Min -|
|Lu, Lei -|
Submitted to: Fungal Biology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: May 4, 2012
Publication Date: July 1, 2012
Repository URL: http://handle.nal.usda.gov/10113/58581
Citation: Han, X., Zhao, M., Lu, L., Liu, Y. 2012. Purification, characterization and decolorization of bilirubin oxidase from Myrothecium verrucaria 3.2190. Fungal Biology. 116(8):863-871. Interpretive Summary: Dyes are intensely colored compounds that have widespread application in the textile industry and can be used for dyeing materials such as nylon, wool, silk, and cotton. Dye decolorization is important in textile industry; however, the different and complicated molecular structures of dyes make them difficult to be treated by conventional physico-chemical methods. Therefore, innovative decoloriztion treatment strategies are needed. Microbial degradation and decolorization of dyes have received considerable attention because of availability and cost effectiveness. This study investigated the potential of an enzyme (bilirubin oxidase) in a fungus for decolorization. The enzyme was purified and characterized and the ability for decolorization was investigated. Information from this study shows that the purified enzyme has potential application in dye effluent decolorization.
Technical Abstract: Myrothecium verrucaria 3.2190 is a nonligninolytic fungus that produces bilirubin oxidase. Both Myrothecium 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 degrees C. Additionally, the crude bilirubin oxidase can efficiently decolorize indigo carmine at 30 degrees C~50 degrees 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 Myrothecium verrucaria strain has potential application in dye effluent decolorization.