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Affinity Electrophoresis as a Method for Determining Substrate-Binding Specificity of Carbohydrate-Active Enzymes for Soluble Polysaccharides

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Biomass Conversion

Part of the book series: Methods in Molecular Biology ((MIMB,volume 908))

Abstract

Affinity electrophoresis is a simple and rapid tool for the analysis of protein-binding affinities to soluble polysaccharides. This approach is particularly suitable for the characterization of the carbohydrate-active enzymes that contain a carbohydrate-binding module and for their mutants and chimeras. Knowledge of the binding characteristics of these enzymes can be the first step to elucidate the enzymatic activity of a putative enzyme; moreover in some cases, enzymes are able to bind polysaccharides targets other than their specified substrate, and this knowledge can be essential to understand the basics of the intrinsic mechanism of these enzymes in their natural environment.

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Authors and Affiliations

  1. Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot, Israel

    Sarah Moraïs & Edward A. Bayer

  2. Department of Molecular Microbiology and Biotechnology, The Daniella Rich Institute for Structural Biology, Tel Aviv University, Ramat Aviv, Israel

    Raphael Lamed

Authors
  1. Sarah Moraïs
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  2. Raphael Lamed
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  3. Edward A. Bayer
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Corresponding author

Correspondence to Edward A. Bayer .

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Editors and Affiliations

  1. , Biosciences Center, National Renewable Energy Laboratory, Cole Boulevard 1617, Golden, 80401-3305, USA

    Michael E. Himmel

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© 2012 Springer Science+Business Media, LLC

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Moraïs, S., Lamed, R., Bayer, E.A. (2012). Affinity Electrophoresis as a Method for Determining Substrate-Binding Specificity of Carbohydrate-Active Enzymes for Soluble Polysaccharides. In: Himmel, M. (eds) Biomass Conversion. Methods in Molecular Biology, vol 908. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-61779-956-3_12

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  • DOI: https://doi.org/10.1007/978-1-61779-956-3_12

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  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-61779-955-6

  • Online ISBN: 978-1-61779-956-3

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