Purification and partial characterization of lignin peroxidase from Acinetobacter calcoaceticus NCIM 2890 and its application in decolorization of textile dyes.
Lignin peroxidase was purified (72-fold) from Acinetobacter calcoaceticus NCIM 2890. The purified lignin peroxidase (55-65 kDa) showed dimeric nature. The maximum enzyme activity was observed at pH 1.0, between a broad temperature range of 50 and 70 degrees C, at H2O2 concentration (40 mM) and the substrate concentration (n-propanol, 100 mM). Purified lignin peroxidase was able to oxidize a variety of substrates including Mn2+, tryptophan, mimosine, L-Dopa, hydroquinone, xylidine, n-propanol, veratryl alcohol, and ten textile dyes of various groups indicating as a versatile peroxidase. Most of the dyes decolorized up to 90%. Tryptophan stabilizes the lignin peroxidase activity during decolorization of dyes.
Department of Biochemistry, Shivaji University, Kolhapur 416004, India.
Gajanan S
GS
Ghodake
Satish D
SD
Kalme
Jyoti P
JP
Jadhav
Sanjay P
SP
Govindwar
D000433:1-Propanol / Q000378:metabolism; D016954:Acinetobacter calcoaceticus / Q000201:enzymology*; D001673:Biodegradation, Environmental; D003116:Color; D004396:Coloring Agents / Q000737:chemistry / Q000378:metabolism*; D004785:Environmental Pollutants / Q000737:chemistry / Q000378:metabolism*; D004795:Enzyme Stability / Q000187:drug effects; D006861:Hydrogen Peroxide / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D010084:Oxidation-Reduction / Q000187:drug effects; D010544:Peroxidases / Q000302:isolation & purification* / Q000378:metabolism*; D013379:Substrate Specificity; D013696:Temperature; D013784:Textiles; D014364:Tryptophan / Q000494:pharmacology
D004396:Coloring Agents; D004785:Environmental Pollutants; D014364:Tryptophan; D000433:1-Propanol; D006861:Hydrogen Peroxide; D010544:Peroxidases; C042858:lignin peroxidase