Purification and characterization of an extracellular laccase from a Pseudomonas sp. LBC1 and its application for the removal of bisphenol A

Amar A. Telke; Dayanand Kalyani; Umesh U. Jadhav; Ganesh K. Parshetti; Sanjay P. Govindwar

doi:10.1016/j.molcatb.2009.08.001

Purification and characterization of an extracellular laccase from a Pseudomonas sp. LBC1 and its application for the removal of bisphenol A

Amar A. Telke, Dayanand Kalyani, Umesh U. Jadhav, Ganesh K. Parshetti, Sanjay P. Govindwar

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

Abstract

The Pseudomonas sp. LBC1 produced extracellular laccase when grown in the nutrient broth. The enzyme was purified using acetone precipitation and an anion-exchange chromatography. The molecular weight of the purified laccase was estimated as 70kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. An enzyme showed maximum substrate specificity towards o-tolidine than other substrates of laccase including 2,2′-azinobis, 3-ethylbenzothiazoline-6-sulfonic acid, hydroquinone, N,N′-dimethyl phenylene diamine, syringic acid and veratryl alcohol. The optimum pH and temperature for the laccase activity were 4.0 and 40°C, respectively. Cyclic voltammogram revealed the redox potential of purified enzyme as 0.30V. The laccase was stable up to 40°C and within pH range 6.0–8.0. Sodium azide and EDTA strongly inhibited laccase activity. The purified laccase completely degraded the higher concentration of bisphenol A within 5h. Biodegradation metabolites of bisphenol A were characterized by using FTIR, HPLC and GC–MS.

Original language	English
Journal	Journal of Molecular Catalysis. B, Enzymatic
Volume	61
Issue number	3-4
Pages (from-to)	252-260
ISSN	1381-1177
DOIs	https://doi.org/10.1016/j.molcatb.2009.08.001
Publication status	Published - 2009
Externally published	Yes

Keywords

Pseudomonas sp. LBC1
Extracellular laccase
Bisphenol A
Biodegradation
Cyclic voltammogram
GC–MS

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title = "Purification and characterization of an extracellular laccase from a Pseudomonas sp. LBC1 and its application for the removal of bisphenol A",

abstract = "The Pseudomonas sp. LBC1 produced extracellular laccase when grown in the nutrient broth. The enzyme was purified using acetone precipitation and an anion-exchange chromatography. The molecular weight of the purified laccase was estimated as 70kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. An enzyme showed maximum substrate specificity towards o-tolidine than other substrates of laccase including 2,2′-azinobis, 3-ethylbenzothiazoline-6-sulfonic acid, hydroquinone, N,N′-dimethyl phenylene diamine, syringic acid and veratryl alcohol. The optimum pH and temperature for the laccase activity were 4.0 and 40°C, respectively. Cyclic voltammogram revealed the redox potential of purified enzyme as 0.30V. The laccase was stable up to 40°C and within pH range 6.0–8.0. Sodium azide and EDTA strongly inhibited laccase activity. The purified laccase completely degraded the higher concentration of bisphenol A within 5h. Biodegradation metabolites of bisphenol A were characterized by using FTIR, HPLC and GC–MS.",

keywords = "Pseudomonas sp. LBC1, Extracellular laccase, Bisphenol A, Biodegradation, Cyclic voltammogram, GC–MS",

author = "Telke, {Amar A.} and Dayanand Kalyani and Jadhav, {Umesh U.} and Parshetti, {Ganesh K.} and Govindwar, {Sanjay P.}",

year = "2009",

doi = "10.1016/j.molcatb.2009.08.001",

language = "English",

volume = "61",

pages = "252--260",

journal = "Journal of Molecular Catalysis - B Enzymatic",

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}

Purification and characterization of an extracellular laccase from a Pseudomonas sp. LBC1 and its application for the removal of bisphenol A. / Telke, Amar A.; Kalyani, Dayanand; Jadhav, Umesh U. et al.

In: Journal of Molecular Catalysis. B, Enzymatic, Vol. 61, No. 3-4, 2009, p. 252-260.

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

TY - JOUR

T1 - Purification and characterization of an extracellular laccase from a Pseudomonas sp. LBC1 and its application for the removal of bisphenol A

AU - Telke, Amar A.

AU - Kalyani, Dayanand

AU - Jadhav, Umesh U.

AU - Parshetti, Ganesh K.

AU - Govindwar, Sanjay P.

PY - 2009

Y1 - 2009

N2 - The Pseudomonas sp. LBC1 produced extracellular laccase when grown in the nutrient broth. The enzyme was purified using acetone precipitation and an anion-exchange chromatography. The molecular weight of the purified laccase was estimated as 70kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. An enzyme showed maximum substrate specificity towards o-tolidine than other substrates of laccase including 2,2′-azinobis, 3-ethylbenzothiazoline-6-sulfonic acid, hydroquinone, N,N′-dimethyl phenylene diamine, syringic acid and veratryl alcohol. The optimum pH and temperature for the laccase activity were 4.0 and 40°C, respectively. Cyclic voltammogram revealed the redox potential of purified enzyme as 0.30V. The laccase was stable up to 40°C and within pH range 6.0–8.0. Sodium azide and EDTA strongly inhibited laccase activity. The purified laccase completely degraded the higher concentration of bisphenol A within 5h. Biodegradation metabolites of bisphenol A were characterized by using FTIR, HPLC and GC–MS.

AB - The Pseudomonas sp. LBC1 produced extracellular laccase when grown in the nutrient broth. The enzyme was purified using acetone precipitation and an anion-exchange chromatography. The molecular weight of the purified laccase was estimated as 70kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. An enzyme showed maximum substrate specificity towards o-tolidine than other substrates of laccase including 2,2′-azinobis, 3-ethylbenzothiazoline-6-sulfonic acid, hydroquinone, N,N′-dimethyl phenylene diamine, syringic acid and veratryl alcohol. The optimum pH and temperature for the laccase activity were 4.0 and 40°C, respectively. Cyclic voltammogram revealed the redox potential of purified enzyme as 0.30V. The laccase was stable up to 40°C and within pH range 6.0–8.0. Sodium azide and EDTA strongly inhibited laccase activity. The purified laccase completely degraded the higher concentration of bisphenol A within 5h. Biodegradation metabolites of bisphenol A were characterized by using FTIR, HPLC and GC–MS.

KW - Pseudomonas sp. LBC1

KW - Extracellular laccase

KW - Bisphenol A

KW - Biodegradation

KW - Cyclic voltammogram

KW - GC–MS

U2 - 10.1016/j.molcatb.2009.08.001

DO - 10.1016/j.molcatb.2009.08.001

M3 - Journal article

VL - 61

SP - 252

EP - 260

JO - Journal of Molecular Catalysis - B Enzymatic

JF - Journal of Molecular Catalysis - B Enzymatic

SN - 1381-1177

IS - 3-4

ER -

Purification and characterization of an extracellular laccase from a Pseudomonas sp. LBC1 and its application for the removal of bisphenol A

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Keywords

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