Biochemical characteristics of a textile dye degrading extracellular laccase from a Bacillus sp. ADR

Amar A. Telke, Gajanan S. Ghodake, Dayanand C. Kalyani, Rhishikesh S. Dhanve, Sanjay P. Govindwar

Research output: Contribution to journalArticlepeer-review

115 Scopus citations

Abstract

Bacillus sp. ADR secretes an extracellular laccase in nutrient broth, and this enzyme was purified up to 56-fold using acetone precipitation and DEAE-cellulose anion exchange chromatography. The molecular weight of purified laccase was estimated to be 66. kDa using sodium dodecyl sulfate polyacrylamide gel electrophoresis. The purified laccase oxidized 2,6-dimethoxy phenol, o-tolidine, hydroquinone, l-DOPA and guaiacol. The optimum pH for oxidation of o-tolidine, 2,6-dimethoxy phenol and guaiacol were 3.0, 4.0 and 5.0, respectively. The purified laccase contained 2.7. mol/mol of copper. The laccase was stable up to 40 °C and within the pH range of 7.0-9.0. Well-known inhibitors of multicopper oxidases such as, sodium azide, l-cysteine and dithiothreitol showed significant inhibition of laccase activity. The purified enzyme decolorized structurally different azo dyes with variable decolorization rates and efficiencies of 68-90%. This study is useful for understanding the precise use of Bacillus sp. ADR in the decolorization of textile dyes containing industrial wastewater.

Original languageEnglish
Pages (from-to)1752-1756
Number of pages5
JournalBioresource Technology
Volume102
Issue number2
DOIs
StatePublished - Jan 2011

Keywords

  • Azo dyes
  • Bacillus sp. ADR
  • Biodegradation
  • Decolorization
  • Laccase

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