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Purification and Partial Characterization of Lignin Peroxidase from Acinetobacter calcoaceticus NCIM 2890 and Its Application in Decolorization of Textile Dyes

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Abstract

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°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.

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Authors and Affiliations

  1. Department of Biochemistry, Shivaji University, Kolhapur, 416004, India

    Gajanan S. Ghodake, Jyoti P. Jadhav & Sanjay P. Govindwar

  2. Department of Chemistry, College of Natural Sciences, Hanyang University, Seoul, 133-791, South Korea

    Satish D. Kalme

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  1. Gajanan S. Ghodake
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  2. Satish D. Kalme
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  3. Jyoti P. Jadhav
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  4. Sanjay P. Govindwar
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Correspondence to Sanjay P. Govindwar.

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Ghodake, G.S., Kalme, S.D., Jadhav, J.P. et al. Purification and Partial Characterization of Lignin Peroxidase from Acinetobacter calcoaceticus NCIM 2890 and Its Application in Decolorization of Textile Dyes. Appl Biochem Biotechnol 152, 6–14 (2009). https://doi.org/10.1007/s12010-008-8258-4

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