TY - JOUR
T1 - Biochemical characteristics of a textile dye degrading extracellular laccase from a Bacillus sp. ADR
AU - Telke, Amar A.
AU - Ghodake, Gajanan S.
AU - Kalyani, Dayanand C.
AU - Dhanve, Rhishikesh S.
AU - Govindwar, Sanjay P.
PY - 2011/1
Y1 - 2011/1
N2 - 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.
AB - 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.
KW - Azo dyes
KW - Bacillus sp. ADR
KW - Biodegradation
KW - Decolorization
KW - Laccase
UR - http://www.scopus.com/inward/record.url?scp=78650693352&partnerID=8YFLogxK
U2 - 10.1016/j.biortech.2010.08.086
DO - 10.1016/j.biortech.2010.08.086
M3 - Article
C2 - 20855194
AN - SCOPUS:78650693352
SN - 0960-8524
VL - 102
SP - 1752
EP - 1756
JO - Bioresource Technology
JF - Bioresource Technology
IS - 2
ER -