Purification and characterization of a bacterial peroxidase from the isolated strain Pseudomonas sp. SUK1 and its application for textile dye decolorization

Dayanand Kalyani; Swapnil S. Phugare; Utkarsha U. Shedbalkar; Jyoti P. Jadhav

doi:10.1007/s13213-010-0162-9

Purification and characterization of a bacterial peroxidase from the isolated strain Pseudomonas sp. SUK1 and its application for textile dye decolorization

Dayanand Kalyani, Swapnil S. Phugare, Utkarsha U. Shedbalkar, Jyoti P. Jadhav

Shivaji University

Research output: Contribution to journal › Journal article › Research › peer-review

Abstract

The intracellular bacterial peroxidase from Pseudomonas sp. SUK1 was purified by anion exchange and molecular sieve chromatography. The molecular weight of the purified peroxidase was estimated to be 86 kDa by SDS-PAGE analysis. The UV-visible absorption spectra revealed that the purified peroxidase was a heme-containing protein. The purified enzyme exerted its optimal activity with n-propanol and also oxidized various lignin-related phenols, whereas no activity was observed with p-cresol and veratrole. Optimum pH and temperature for the purified peroxidase were 3.0 and 40°C, respectively. The purified enzyme proficiently decolorized various textile dyes. Methyl orange was used as a model azo dye to understand the mechanism of action of peroxidase in dye degradation. Further, dye degradation was confirmed by analytical techniques like FTIR, HPLC and GC-MS.

Original language	English
Journal	Annals of Microbiology
Volume	61
Issue number	3
Pages (from-to)	483-491
ISSN	1590-4261
DOIs	https://doi.org/10.1007/s13213-010-0162-9
Publication status	Published - 2011
Externally published	Yes

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title = "Purification and characterization of a bacterial peroxidase from the isolated strain Pseudomonas sp. SUK1 and its application for textile dye decolorization",

abstract = "The intracellular bacterial peroxidase from Pseudomonas sp. SUK1 was purified by anion exchange and molecular sieve chromatography. The molecular weight of the purified peroxidase was estimated to be 86 kDa by SDS-PAGE analysis. The UV-visible absorption spectra revealed that the purified peroxidase was a heme-containing protein. The purified enzyme exerted its optimal activity with n-propanol and also oxidized various lignin-related phenols, whereas no activity was observed with p-cresol and veratrole. Optimum pH and temperature for the purified peroxidase were 3.0 and 40°C, respectively. The purified enzyme proficiently decolorized various textile dyes. Methyl orange was used as a model azo dye to understand the mechanism of action of peroxidase in dye degradation. Further, dye degradation was confirmed by analytical techniques like FTIR, HPLC and GC-MS.",

author = "Dayanand Kalyani and Phugare, {Swapnil S.} and Shedbalkar, {Utkarsha U.} and Jadhav, {Jyoti P.}",

year = "2011",

doi = "10.1007/s13213-010-0162-9",

language = "English",

volume = "61",

pages = "483--491",

journal = "Annals of Microbiology",

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publisher = "Springer",

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Purification and characterization of a bacterial peroxidase from the isolated strain Pseudomonas sp. SUK1 and its application for textile dye decolorization. / Kalyani, Dayanand; Phugare, Swapnil S.; Shedbalkar, Utkarsha U. et al.

In: Annals of Microbiology, Vol. 61, No. 3, 2011, p. 483-491.

Research output: Contribution to journal › Journal article › Research › peer-review

TY - JOUR

T1 - Purification and characterization of a bacterial peroxidase from the isolated strain Pseudomonas sp. SUK1 and its application for textile dye decolorization

AU - Kalyani, Dayanand

AU - Phugare, Swapnil S.

AU - Shedbalkar, Utkarsha U.

AU - Jadhav, Jyoti P.

PY - 2011

Y1 - 2011

N2 - The intracellular bacterial peroxidase from Pseudomonas sp. SUK1 was purified by anion exchange and molecular sieve chromatography. The molecular weight of the purified peroxidase was estimated to be 86 kDa by SDS-PAGE analysis. The UV-visible absorption spectra revealed that the purified peroxidase was a heme-containing protein. The purified enzyme exerted its optimal activity with n-propanol and also oxidized various lignin-related phenols, whereas no activity was observed with p-cresol and veratrole. Optimum pH and temperature for the purified peroxidase were 3.0 and 40°C, respectively. The purified enzyme proficiently decolorized various textile dyes. Methyl orange was used as a model azo dye to understand the mechanism of action of peroxidase in dye degradation. Further, dye degradation was confirmed by analytical techniques like FTIR, HPLC and GC-MS.

AB - The intracellular bacterial peroxidase from Pseudomonas sp. SUK1 was purified by anion exchange and molecular sieve chromatography. The molecular weight of the purified peroxidase was estimated to be 86 kDa by SDS-PAGE analysis. The UV-visible absorption spectra revealed that the purified peroxidase was a heme-containing protein. The purified enzyme exerted its optimal activity with n-propanol and also oxidized various lignin-related phenols, whereas no activity was observed with p-cresol and veratrole. Optimum pH and temperature for the purified peroxidase were 3.0 and 40°C, respectively. The purified enzyme proficiently decolorized various textile dyes. Methyl orange was used as a model azo dye to understand the mechanism of action of peroxidase in dye degradation. Further, dye degradation was confirmed by analytical techniques like FTIR, HPLC and GC-MS.

U2 - 10.1007/s13213-010-0162-9

DO - 10.1007/s13213-010-0162-9

M3 - Journal article

VL - 61

SP - 483

EP - 491

JO - Annals of Microbiology

JF - Annals of Microbiology

SN - 1590-4261

IS - 3

ER -

Purification and characterization of a bacterial peroxidase from the isolated strain Pseudomonas sp. SUK1 and its application for textile dye decolorization

Abstract

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