Peroxidase from Bacillus sp. VUS and its role in the decolorization of textile dyes

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%

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

Olajuyigbe¹,

Ehiosun²,

Jaiyesimi³

2015

AER

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“…Lignin peroxidase catalyzes the oxidative breakdown of azo dye Disperse orange 3, resulting in the formation of nitrobenzene as a major product (Zhao et al 2006). The role of purified lignin peroxidase in the degradation of azo dyes like Methyl orange and Methyl red has also been reported (Gomare et al 2008;Dawkar et al 2009;Ghodake et al 2009). …”

Section: Introductionmentioning

confidence: 88%

“…Earlier reports on bacterial peroxidases purified from Bacillus sp. VUS (Dawkar et al 2009) and Acinetobacter calcoaceticus NCIM 2890 (Ghodake et al 2009) showed molecular weights of 43 kDa and 110 kDa, respectively. Figure 4 shows the effects of pH and temperature on peroxidase activity.…”

Section: Characterization Of Purified Peroxidasementioning

confidence: 99%

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

et al. 2010

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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.

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“…Peroxidase oxidized n-propanol much faster as compared to other substrates (hydroxyquinone, L-DOPA and veratrole) which are phenolic and aromatic compounds. The K m and V max values for peroxidase with n-propanol as a substrate were found to be 0.076 mM and 3 9 10 2 lM, respectively (Dawkar et al 2009). The presence of H 2 O 2 showed an increase in the peroxidase activity by 1.33-fold, with Km 0.046 mM for H 2 O 2 (Fig.…”

Section: Enzyme Activities While Decolorization In Batch Culturementioning

confidence: 99%

Effect of inducers on the decolorization and biodegradation of textile azo dye Navy blue 2GL by Bacillus sp. VUS

et al. 2009

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Bacillus sp. VUS decolorized azo dye Navy blue 2GL in 48 h at static anoxic condition in yeast extract medium, whereas it took only 18 h for the decolorization in presence of CaCl(2). Different inducers played role in the decolorization of Navy blue 2GL. CaCl(2) found to be the most effective inducer among all inducers tested. The activity of enzymes like lignin peroxidase, laccase and reductases viz. NADH-DCIP, azo and riboflavin induced during decolorization represents their role in the biodegradation. Extracellular LiP and intracellular laccase activity induced with CaCl(2). Yeast extract was best medium for faster decolorization than other media. UV-vis spectrophotometer analysis and visual examinations showed decolorization of dye. High performance liquid chromatography, Fourier transforms infrared spectroscopy showed degradation of dye. Gas Chromatography-Mass Spectroscopy revealed formation of 4-Amino-3-(2-bromo-4, 6-dinitro-phenylazo)-phenol and acetic acid 2-(-acetoxy-ethylamino)-ethyl ester as final products. Bacillus sp. VUS also decolorized synthetic effluent. Phytotoxicity study showed detoxification of Navy blue 2GL.

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Peroxidase from Bacillus sp. VUS and its role in the decolorization of textile dyes

Cited by 38 publications

References 31 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 a bacterial peroxidase from the isolated strain Pseudomonas sp. SUK1 and its application for textile dye decolorization

Effect of inducers on the decolorization and biodegradation of textile azo dye Navy blue 2GL by Bacillus sp. VUS

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