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  Metaproteome analysis of sewage sludge from membrane bioreactors

Kuhn, R., Benndorf, D., Rapp, E., Reichl, U., Palese, L., & Pollice, A. (2011). Metaproteome analysis of sewage sludge from membrane bioreactors. Proteomics, 11(13), 2738-2744. doi:10.1002/pmic.201000590.

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Kuhn, R.1, 2, 3, Autor
Benndorf, D.4, Autor           
Rapp, E.5, Autor           
Reichl, U.4, 5, Autor           
Palese, L.2, Autor
Pollice, A.1, Autor
Affiliations:
1IRSA CNR, Water Research Institute, Bari, Italy, ou_persistent22              
2University of Bari, Department of Medical Biochemistry, Biology and Physics, Policlinico, Bari, Italy, ou_persistent22              
3BTU Cottbus, Department of Biotechnology of Wastewater Treatment, Cottbus, Germany, ou_persistent22              
4Otto-von-Guericke-Universität Magdeburg, ou_1738156              
5Bioprocess Engineering, Max Planck Institute for Dynamics of Complex Technical Systems, Max Planck Society, ou_1738140              

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Schlagwörter: De novo sequencing, Membrane bioreactor, Metaproteomics, Microbial communities, Microbiology, Protein extraction
 Zusammenfassung: Microbial dynamics and enzymatic activities of activated sludge processes are not completely understood yet. A better understanding about the biology is indispensable for further process optimization. Since proteins play a key role as catalysts in sludge processes, a protocol for protein extraction and analysis by 2-D PAGE was established. It is based on phenol extraction of alkaline extracts and on a subsequent precipitation with ammonium sulphate. 2-D protein patterns obtained from different sludges collected from membrane bioreactors showed – besides common spots – significant differences. Selected proteins were identified with nano-HPLC-ESI-MS/MS. All membrane biological reactor (MBR) sludge samples investigated in this study contained elastase 3A, which implies that this human serine protease is a significant constituent of municipal wastewater. Although the identification of proteins from ammonia-oxidizing bacterium Nitrosomonas europaea was expected, the detection of a protein with homology to the marine bacterium Saprospira grandis in MBR1 was surprising. copyright 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim [accessed July 28th 2011]

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Sprache(n): eng - English
 Datum: 2011
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 570605
DOI: 10.1002/pmic.201000590
 Art des Abschluß: -

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Titel: Proteomics
Genre der Quelle: Zeitschrift
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Affiliations:
Ort, Verlag, Ausgabe: Weinheim, Fed. Rep. of Germany : WILEY-VCH Verlag
Seiten: - Band / Heft: 11 (13) Artikelnummer: - Start- / Endseite: 2738 - 2744 Identifikator: ISSN: 1615-9853
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000294310