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Purification and cellulosomal localization ofClostridium thermocellum mixed linkage β-glucanase LicB (1,3–1,4-β-D-glucanase)

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Summary

Clostridium thermocellum recombinant β-(1,3–1,4)-glucanase LicB was expressed inEscherichia coli K-12 and purified to electrophoretic homogeneity. Specific activity of the final preparation was 12,000 U/mg. Antibodies against recombinant LicB protein reacted with a specific band of purifiedC. thermocellum F7 cellulosomes, suggesting localization in the extracellular multienzyme complex. This indicates that the cellulosome takes part in the hydrolysis of other polysaccharides besides cellulose.

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Authors and Affiliations

  1. Institute of Molecular Genetics, Russian Academy of Sciences, Kurchatov sq. 46, 123182, Moscow, Russia

    V. V. Zverlov & G. A. Velikodvorskaya

  2. Institute for Microbiology, Technical University of Munich, Arcisstr. 21, D-80290, Muenchen, Germany

    K. P. Fuchs & W. H. Schwarz

Authors
  1. V. V. Zverlov
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  2. K. P. Fuchs
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  3. W. H. Schwarz
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  4. G. A. Velikodvorskaya
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Zverlov, V.V., Fuchs, K.P., Schwarz, W.H. et al. Purification and cellulosomal localization ofClostridium thermocellum mixed linkage β-glucanase LicB (1,3–1,4-β-D-glucanase). Biotechnol Lett 16, 29–34 (1994). https://doi.org/10.1007/BF01022619

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