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Induced differential metaproteomics: identification of thermostable cellulases in a methanogenic microbial community
Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, The Institute of Technology. (Molecular Biotechnology)
Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, The Institute of Technology. (Molecular Biotechnology)
Linköping University, Department of Physics, Chemistry and Biology, Chemistry. Linköping University, The Institute of Technology. (Molecular Biotechnology)
2014 (English)Conference paper, Poster (with or without abstract) (Other academic)
Abstract [en]

The identification of novel enzymes for use in industrial biotechnology is an important goal in enzyme discovery. Most industrially relevant enzymes to date have been isolated from pure cultured microorganisms. For future discovery of novel enzymes this is however a major bottleneck since it is well established that only a small fraction of all microorganisms can be obtained in pure cultures. The possibility to identify enzymes directly from complete microbial communities would therefore give access to a huge number of novel enzyme candidates.

Metaproteomics has hitherto mainly been used to understand ecosystem functions. We have instead used the dynamics of proteomics to develop a method based on “induced differential metaproteomics”, by which a desired enzyme activity is induced in a full microbial population and compared to a non-induced reference of the very same population. In a first example the goal was to induce, select and identify cellulases from a thermophilic methanogenic community.

Out of several hundred detectable proteins in a 2D-DIGE experiment, 24 proteins could be identified as at least two-fold up-regulated upon induction. For some proteins spots, the cellulolytic activity was further validated by activity staining using 2D-zymography. Mass spectrometry analysis revealed that 21 out of the 24 up-regulated proteins are cellulases or associated to cellulolytic activity giving a remarkable hit-rate of 88%. This demonstrates the high efficiency and precision of the method, by which a much wider span of the microbial world can be scanned for novel and targeted enzymes.

Place, publisher, year, edition, pages
2014.
Keyword [en]
industrial biotechnology; metaproteomics; cellulases; methanogenic; microbial community; induction; enzyme activity; 2D-DIGE; mass spectrometry
National Category
Biocatalysis and Enzyme Technology
Identifiers
URN: urn:nbn:se:liu:diva-133030OAI: oai:DiVA.org:liu-133030DiVA: diva2:1052935
Conference
16th European Congress on Biotechnology, 13-16 July 2014, Edinburgh, Scotland
Available from: 2016-12-07 Created: 2016-12-07 Last updated: 2016-12-15Bibliographically approved

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Speda, JuttaJonsson, Bengt-HaraldKarlsson, Martin
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CiteExportLink to record
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Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Other style
More styles
Language
  • de-DE
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