A catalase-peroxidase from a newly isolated thermoalkaliphilic Bacillus sp. with potential for the treatment of textile bleaching effluents

Gudelj, Marinka; Fruhwirth, Gilbert O.; Paar, Andreas; Lottspeich, F.; Robra, Karl‐Heinz; Cavaco-Paulo, Artur; Gübitz, Georg

doi:10.1007/s007920100218

Cited by 50 publications

(35 citation statements)

References 32 publications

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“…In this study we have shown that the P. furiosus protein has rubredoxin-dependent peroxidase activity, which is comparable to that reported for archaeal and bacterial (nonrubrerythrin) peroxidases, such as from Archaeoglobus fulgidus (25), Thermus brockianus (45), Bacillus stearothermophilus (17), and Halobacterium halobium (5). The gene encoding rubrerythrin is adjacent to those encoding rubredoxin and superoxide reductase in the P. furiosus genome, consistent with a functional relationship between them (23).…”

Section: Discussionsupporting

confidence: 85%

Rubrerythrin from the Hyperthermophilic Archaeon Pyrococcus furiosus Is a Rubredoxin-Dependent, Iron-Containing Peroxidase

et al. 2004

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Rubrerythrin was purified by multistep chromatography under anaerobic, reducing conditions from the hyperthermophilic archaeon Pyrococcus furiosus. It is a homodimer with a molecular mass of 39.2 kDa and contains 2.9 ؎ 0.2 iron atoms per subunit. The purified protein had peroxidase activity at 85°C using hydrogen peroxide with reduced P. furiosus rubredoxin as the electron donor. The specific activity was 36 mol of rubredoxin oxidized/min/mg with apparent K m values of 35 and 70 M for hydrogen peroxide and rubredoxin, respectively. When rubrerythrin was combined with rubredoxin and P. furiosus NADH:rubredoxin oxidoreductase, the complete system used NADH as the electron donor to reduce hydrogen peroxide with a specific activity of 7.0 mol of H 2 O 2 reduced/min/mg of rubrerythrin at 85°C. Strangely, as-purified (reduced) rubrerythrin precipitated when oxidized by either hydrogen peroxide, air, or ferricyanide. The gene (PF1283) encoding rubrerythrin was expressed in Escherichia coli grown in medium with various metal contents. The purified recombinant proteins each contained approximately three metal atoms/subunit, ranging from 0.4 Fe plus 2.2 Zn to 1.9 Fe plus 1.2 Zn, where the metal content of the protein depended on the metal content of the E. coli growth medium. The peroxidase activities of the recombinant forms were proportional to the iron content. P. furiosus rubrerythrin is the first to be characterized from a hyperthermophile or from an archaeon, and the results are the first demonstration that this protein functions in an NADH-dependent, hydrogen peroxide: rubredoxin oxidoreductase system. Rubrerythrin is proposed to play a role in the recently defined anaerobic detoxification pathway for reactive oxygen species.

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Section: Discussionsupporting

confidence: 85%

Rubrerythrin from the Hyperthermophilic Archaeon Pyrococcus furiosus Is a Rubredoxin-Dependent, Iron-Containing Peroxidase

et al. 2004

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“…strain SF decolorizes a number of azo dyes. This activity, however, cannot be attributed to the catalase-peroxidase previously isolated from this organism, which did not attack any of the tested dyes (13). An intracellular azoreductase (EC 1.7.1.6 [azobenzene reductase]) is responsible for the decolorization activity, as previously shown for other azo-dye-degrading microorganisms (11,31,36).…”

Section: Discussionsupporting

confidence: 53%

A New Alkali-Thermostable Azoreductase from Bacillus sp. Strain SF

Maier

Kandelbauer

Erlacher

et al. 2004

Appl Environ Microbiol

217

100

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A screening for dye-decolorizing alkali-thermophilic microorganisms resulted in a Bacillus sp. strain isolated out of the wastewater drain of a textile finishing company. An NADH-dependent azoreductase of this strain, Bacillus sp. strain SF, was found to be responsible for the decolorization of azo dyes. This enzyme was purified by a combination of ammonium sulfate precipitation and anion-exchange and affinity chromatography and had a molecular mass of 61.6 kDa and an isoelectric point at pH 5.3. The pH optimum of the azoreductase depended on the substrate and was within the range of pHs 8 to 9, while the temperature maximum was reached at 80°C. Decolorization only took place in the absence of oxygen and was enhanced by FAD, which was not consumed during the reaction. A 26% similarity of this azoreductase to chaperonin Cpn60 from a Bacillus sp. was found by peptide mass mapping experiments. Substrate specificities of the azoreductase were studied by using synthesized model substrates based on di-sodium-(R)-benzyl-azo-2,7-dihydroxy-3,6-disulfonyl-naphthaline. Those dyes with NO 2 substituents, especially in the ortho position, were degraded fastest, while analogues with a methyl substitution showed the lowest degradation rates.In the last few years, environmental legislation, e.g., about the appearance of color in discharges, combined with the increasing cost of water for the industrial sector, has made the treatment and reuse of dyeing effluents increasingly attractive to the industry. The common method for the treatment of wastewater in the textile finishing industry is physicochemical flocculation in combination with biological treatment (17). The conventional treatment of colored effluents produces a lot of sludge, but does not remove all dyes, thus preventing recycling of the treated wastewater. In activated sludge treatments, dyeing effluents, e.g., reactive azo dyes and naphthaline-sulfonic acids as well as aromatic amino derivatives, represent an extensive nonbiodegradable class of compounds (18) and can even inhibit activated sludge organisms. Thus, the development of more effective biological systems for the treatment of these types of wastewater has resulted in considerable interest by the industry.Wood-rotting fungi (e.g., Phanerochaete chrysosporium, Trametes sp., and Aspergillus sp.) have been found to effectively degrade a variety of azo dyes under aerobic conditions (16). Dye-degrading fungi have been used frequently in bioreactors for the decolorization and degradation of azo dyes (37). While fungal treatment of effluents is usually very time-consuming (3), immobilized enzymes could have potential for dye decolorization and recycling of effluents (1) without the need for the addition of growth substrates. The enzymes involved in the degradation of azo dyes are mainly peroxidases (12) and laccases (1). However, a significant cost reduction for these enzymes would be required in order to make this process economically more attractive. Aerobic bacteria have been described to oxidatively decolorize m...

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“…These observed half life times indicate a high potential for industrial processes like dye decolorization, detoxification, and transformation of phenolic and other compounds where high temperatures and pH values are common. Previously, an intracellular catalase-peroxide from this Bacillus SF has been described which also showed high stabilities at alkaline pH and high temperatures (Gudelj et al 2001). …”

Section: Ph Stabilitiesmentioning

confidence: 97%

“…Bacillus SF was isolated as described previously (Gudelj et al 2001). Cultures were grown on Caso-agar (Merck) plates pH adjusted with NaOH to 8.5 for 2 days at 55 • C and thereafter stored at 4 • C. The medium for liquid cultivation of Bacillus SF consisted of two different solutions which were combined after autoclaving.…”

Section: Cultivation Of Bacillus Sfmentioning

confidence: 99%

Biotransformation of phenolics with laccase containing bacterial spores

et al. 2005

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Treatment of effluents containing phenols such as textile dyes with fungal laccases is usually limited to the acid to neutral pH range and moderate temperatures. Here we demonstrate for the first time that spore-bound laccases which are stable at high temperatures and pH values can be used for phenolic dye decolorisation. Laccase containing spores from Bacillus SF were immobilized on alumina pellets. Both immobilized and free spores were able to completely decolorize the common textile dyes Mordant Black 9, Mordant Brown 96/Mordant Brown 15, and Acid Blue 74 within 90 min of incubation time and decolorized solutions were successfully used in re-dyeing.

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A catalase-peroxidase from a newly isolated thermoalkaliphilic Bacillus sp. with potential for the treatment of textile bleaching effluents

Cited by 50 publications

References 32 publications

Rubrerythrin from the Hyperthermophilic Archaeon Pyrococcus furiosus Is a Rubredoxin-Dependent, Iron-Containing Peroxidase

Rubrerythrin from the Hyperthermophilic Archaeon Pyrococcus furiosus Is a Rubredoxin-Dependent, Iron-Containing Peroxidase

A New Alkali-Thermostable Azoreductase from Bacillus sp. Strain SF

Biotransformation of phenolics with laccase containing bacterial spores

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