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.; Jadhav, Jyoti P.

doi:10.1007/s13213-010-0162-9

Cited by 53 publications

(51 citation statements)

References 35 publications

(39 reference statements)

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“…SUK1 and Bacillus sp. VUS had optimum pH of 3.0 [26] [27]. Our present studies show that actinobacterial POXs have optimum pH of 7.0.…”

Section: Effect Of Ph On Total Pox Activity and Stabilitysupporting

confidence: 52%

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Preliminary Study towards Enhanced Crude Oil Biodegradation Reveals Congeneric Total Peroxidases with Striking Distinctions

Olajuyigbe¹,

Ehiosun²,

Jaiyesimi³

2015

AER

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Peroxidases (POXs) are the key extracellular enzymes produced by crude oil degrading microbes. Knowledge of optimum conditions for POXs activity is crucial for providing effective environment for bioremediation. In this study, physicochemical properties of POXs produced by Actinomyces israelii and Actinomyces viscosus during growth on crude oil were studied. The POXs exhibited similarities in activity and stability with striking differences in response to two divalent metal ions. The POXs from both species had optimum pH of 7.0 and were very stable over a narrow pH range (6.0 -8.0). The POXs demonstrated similar thermostability exhibiting relative residual activity of 62% at 50˚C after 30 min incubation and 45% residual activity at the same temperature after 60 min despite the fact that POXs from A. viscosus and A. israelii had optimum temperatures of 50˚C and 40˚C, respectively. The POXs from A. viscosus and A. israelii were greatly activated by Fe 2+ at 5.0 and 10.0 mM. The enzymes were both strongly inhibited by Cu 2+ , Mg 2+ and Hg 2+ . Surprisingly, these congeneric POXs demonstrated striking differences in their response to Ca 2+ and Mn 2+ . POX from A. viscosus was activated by Ca 2+ and Mn 2+ exhibiting relative activity of 136% and 106% at 5 mM, respectively. In contrast, POX from A. israelii was strongly inhibited by Ca 2+ and Mn 2+ exhibiting 62.5% relative activity in the presence of 5 mM of each metal ion. Increasing the concentration of Ca 2+ and Mn 2+ led to further activation of POX from A. viscosus and inhibition of POX from A. israelii. Results provide deeper insights into functional properties of studied POXs from closely related microbes. The physicochemical properties are very similar; however, notable differences provide a strong basis for structural characterization of these congeneric enzymes.

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“…SUK1 and Bacillus sp. VUS had optimum pH of 3.0 [26] [27]. Our present studies show that actinobacterial POXs have optimum pH of 7.0.…”

Section: Effect Of Ph On Total Pox Activity and Stabilitysupporting

confidence: 52%

“…Similar finding was reported on the bacterial POX from Pseudomonas sp. SUK1 which was optimally active at 40˚C [26]. Lower optimum temperatures of 25˚C and 35˚C have been reported for POXs from B. pumilus and Paenibacillus sp.…”

Section: Effect Of Temperature On Total Pox Activity and Stabilitymentioning

confidence: 83%

Preliminary Study towards Enhanced Crude Oil Biodegradation Reveals Congeneric Total Peroxidases with Striking Distinctions

Olajuyigbe¹,

Ehiosun²,

Jaiyesimi³

2015

AER

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“…Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was performed according to previous protocol (Kalyani et al 2010) with 4% stacking gel and 12% separating gel using a vertical gel electrophoresis system (GeNei, Bangalore, India). Similarly, protein with oxidase activity was evaluated using non denaturing PAGE electrophoresis (12% separating and 4% stacking gel).…”

Section: Polyacrylamide Gel Electrophoresis (Page) Analysismentioning

confidence: 99%

“…Oxidases are capable of oxidizing variety of xenobiotic compounds including polycyclic aromatic hydrocarbons, polychlorinated phenols, nitroaromatics, and azo dyes (Jadhav et al 2008). Similar to oxidases, various peroxidases are also reported for the dye decolorization Kalyani et al 2010). Laccases are oxidoreductases that have potential in various biotechnological processes, mainly due to their high non-specific oxidation capacity, lack of a requirement for cofactors and use of readily available oxygen as an electron acceptor (Sharma et al 2007).…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of dye degrading of veratryl alcohol oxidase from Pseudomonas aeruginosa strain BCH

Phugare

Waghmare

Jadhav

2011

World J Microbiol Biotechnol

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In the present study we have purified the intracellular veratryl alcohol oxidase (VAO) enzyme from Pseudomonas aeruginosa strain BCH to evaluate its dye decolorizing potential. The enzyme was purified by ion exchange chromatography using DEAE cellulose followed by gel filtration chromatography using Biogel P-100. The molecular weight of the purified enzyme was estimated by polyacrylamide gel electrophoresis (PAGE) analysis. The VAO was purified up to 12 and 16.3-fold by ion exchange and gel filtration chromatography respectively. VAO was estimated to be about 85 kDa by SDS-PAGE. The optimum pH and temperature for purified VAO was 3 and 55°C respectively. The purified enzyme exerted its optimal activity with veratryl alcohol and also oxidized various other substrates, whereas diminished activity was noted in case of tryptophan and xylidine. The metal ions Mn ?? and Hg ?? were found to suppress the oxidase activity. The purified enzyme decolorized different dyes with variable decolorization rates and efficiencies. Decolorization mechanism of Remazol Black by purified enzyme was studies in detail using various analytical techniques like HPLC, GC-MS and FTIR. This study is useful for understanding the precise role of Pseudomonas aeruginosa strain BCH in the decolorization of textile dyes containing industrial wastewater.

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“…Among these 10 isolates, 4 isolate selected for further quantitative assay for Lignin Modifying Enzymes (LME) i.e., laccase, LiP and MnP. Isolate 72 showed higher laccase (453.6), LiP (95.0) (Kalyani et al, 2008). Cellulolytic microbes can convert cellulose in to soluble sugars by enzymatic hydrolysis.…”

Section: Issn: 2319-7706 Volume 6 Number 12 (2017) Pp 3808-3816mentioning

confidence: 99%

Exploring Microbes for their Cellulolytic and Lignolytic Enzyme Activity for Manure Preparation

Madhavan¹,

Patel²,

Vyas³

et al. 2017

Int.J.Curr.Microbiol.App.Sci

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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

Cited by 53 publications

References 35 publications

Preliminary Study towards Enhanced Crude Oil Biodegradation Reveals Congeneric Total Peroxidases with Striking Distinctions

Preliminary Study towards Enhanced Crude Oil Biodegradation Reveals Congeneric Total Peroxidases with Striking Distinctions

Purification and characterization of dye degrading of veratryl alcohol oxidase from Pseudomonas aeruginosa strain BCH

Exploring Microbes for their Cellulolytic and Lignolytic Enzyme Activity for Manure Preparation

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