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

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons78335

Lottspeich,  F.
Lottspeich, Friedrich / Protein Analysis, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

Gudelj, M., Fruhwirth, G. O., Paar, A., Lottspeich, F., Robra, K. H., Cavaco-Paulo, A., et al. (2001). A catalase-peroxidase from a newly isolated thermoalkaliphilic Bacillus sp with potential for the treatment of textile bleaching effluents. Extremophiles, 5(6), 423-429.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-70EE-5
Zusammenfassung
A new thermoalkaliphilic bacterium was isolated from a textile wastewater drain and identified as a new Bacillus sp. (Bacillus SF). Because of its high pH stability and thermostability, a catalase-peroxidase (CP) from this strain has potential for the treatment of textile bleaching effluents. The CP from Bacillus SF was purified to more than 70.3-fold homogeneity using fractionated ammonium sulfate precipitation, hydrophobic interaction, and anion-exchange and gel-filtration chromatography. The native CP had a molecular mass of 165 kDa and was composed of two identical subunits. The isoelectric point of the protein was at pH 6.0. Peptide mass mapping using matrix-assisted laser desorption ionization-mass spectrometry showed a homology between the CP from Bacillus SF and the CP from Bacillus stearothermophilus. The apparent K-m value of the catalase activity for H2O2 was 2.6 mM and the k(cat) value was 11,475 s(-1). The enzyme showed high catalase activity and an appreciable peroxidase activity with guaiacol and o- dianisidine. The enzyme was stable at high pH, with a half-life of 104 h at pH 10 and 25 degreesC and 14 h at 50 degreesC. The enzyme was inhibited by azide and cyanide, in a competitive manner, but not by the catalase-specific inhibitor 3-amino- 1,2,4-triazole.