Purification and partial characterization of lignin peroxidase from Acinetobacter calcoaceticus NCIM 2890 and its application in decolorization of textile dyes

Gajanan S. Ghodake; Satish D. Kalme; Jyoti P. Jadhav; Sanjay P. Govindwar

doi:10.1007/s12010-008-8258-4

Purification and partial characterization of lignin peroxidase from Acinetobacter calcoaceticus NCIM 2890 and its application in decolorization of textile dyes

Gajanan S. Ghodake, Satish D. Kalme, Jyoti P. Jadhav, Sanjay P. Govindwar

Department of Biological and Environmental Science

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89 Scopus citations

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.

Original language	English
Pages (from-to)	6-14
Number of pages	9
Journal	Applied Biochemistry and Biotechnology
Volume	152
Issue number	1
DOIs	https://doi.org/10.1007/s12010-008-8258-4
State	Published - Jan 2009

Keywords

Acinetobacter calcoaceticus
Biodegradation
Lignin peroxidase
Textile dyes
Tryptophan

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10.1007/s12010-008-8258-4

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title = "Purification and partial characterization of lignin peroxidase from Acinetobacter calcoaceticus NCIM 2890 and its application in decolorization of textile dyes",

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.",

keywords = "Acinetobacter calcoaceticus, Biodegradation, Lignin peroxidase, Textile dyes, Tryptophan",

author = "Ghodake, {Gajanan S.} and Kalme, {Satish D.} and Jadhav, {Jyoti P.} and Govindwar, {Sanjay P.}",

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language = "English",

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Purification and partial characterization of lignin peroxidase from Acinetobacter calcoaceticus NCIM 2890 and its application in decolorization of textile dyes. / Ghodake, Gajanan S.; Kalme, Satish D.; Jadhav, Jyoti P. et al.
In: Applied Biochemistry and Biotechnology, Vol. 152, No. 1, 01.2009, p. 6-14.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Purification and partial characterization of lignin peroxidase from Acinetobacter calcoaceticus NCIM 2890 and its application in decolorization of textile dyes

AU - Ghodake, Gajanan S.

AU - Kalme, Satish D.

AU - Jadhav, Jyoti P.

AU - Govindwar, Sanjay P.

PY - 2009/1

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N2 - 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.

AB - 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.

KW - Acinetobacter calcoaceticus

KW - Biodegradation

KW - Lignin peroxidase

KW - Textile dyes

KW - Tryptophan

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JF - Applied Biochemistry and Biotechnology

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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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