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

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

Research output: Contribution to journalJournal articleResearchpeer-review


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 66kDa 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 2.7mol/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
JournalBioresource Technology
Issue number2
Pages (from-to)1752-1756
Publication statusPublished - 2011
Externally publishedYes


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


Dive into the research topics of 'Biochemical characteristics of a textile dye degrading extracellular laccase from a Bacillus sp. ADR'. Together they form a unique fingerprint.

Cite this