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

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.

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Genre: Journal Article
Alternative Title : Extremophiles

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 Creators:
Gudelj, M., Author
Fruhwirth, G. O., Author
Paar, A., Author
Lottspeich, F.1, Author           
Robra, K. H., Author
Cavaco-Paulo, A., Author
Gubitz, G. M., Author
Affiliations:
1Lottspeich, Friedrich / Protein Analysis, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565158              

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Free keywords: thermostable; alkalistable; Baccilus sp.; catalase; peroxidase; textile bleaching
 Abstract: 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.

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Language(s): eng - English
 Dates: 2001-12
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 34939
ISI: 000172837600008
 Degree: -

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Title: Extremophiles
  Alternative Title : Extremophiles
Source Genre: Journal
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Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 5 (6) Sequence Number: - Start / End Page: 423 - 429 Identifier: ISSN: 1431-0651