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Description of a cellulose-binding domain and a linker sequence from Aspergillus fungi

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Abstract.

A family I cellulose-binding domain (CBD) and a serine- and threonine-rich linker peptide were cloned from the fungi Aspergillus japonicus and Aspergillus aculeatus. A glutathione S-transferase (GST) fusion protein comprising GST and a peptide linker with the CBD fused to its C-terminus, was expressed in Escherichia coli. The renatured GST-CBD recovered from inclusion bodies had a molecular mass of 36.5 kDa which agrees with the 29 kDa of the GST plus the calculated 7.5 kDa of the linker with the CBD. The isolated GST-CBD protein adsorbed to both bacterial microcrystalline cellulose and carboxymethyl cellulose. Deletion of the linker peptide caused a decrease in cellulose adsorbance and a higher sensitivity to protease digestion.

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Authors and Affiliations

  1. Department of Fibre and Paper Technology, ATO BV, PO Box 17, 6700 AA Wageningen, The Netherlands, , , , ,

    M. Quentin &  H. van der Valk

  2. Department of Pharmaceutical Biology, University of Groningen, PO Box 72, 9700 AB Groningen, The Netherlands, , , , ,

    M. Ebbelaar

  3. Department of Experimental Botany, Catholic University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands, , , , ,

    J. Derksen &  C. Mariani

Authors
  1. M. Quentin
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  2. M. Ebbelaar
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  3. J. Derksen
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  4. C. Mariani
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  5. H. van der Valk
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Quentin, .M., Ebbelaar, .M., Derksen, .J. et al. Description of a cellulose-binding domain and a linker sequence from Aspergillus fungi. Appl Microbiol Biotechnol 58, 658–662 (2002). https://doi.org/10.1007/s00253-002-0937-4

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  • DOI: https://doi.org/10.1007/s00253-002-0937-4

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