Investigation of cellobiohydrolase from trichoderma reesei by small angle X-ray scattering

@article{Schmuck2005InvestigationOC,
  title={Investigation of cellobiohydrolase from trichoderma reesei by small angle X-ray scattering},
  author={Maria Schmuck and Ingrid Pilz and Marianne Hayn and Hermann Esterbauer},
  journal={Biotechnology Letters},
  year={2005},
  volume={8},
  pages={397-402}
}
  • Maria Schmuck, Ingrid Pilz, +1 author Hermann Esterbauer
  • Published 2005
  • Biology
  • Biotechnology Letters
  • SummaryTrichoderma reesei was grown on sulfite pulp and the major cellobiohydrolase of the culture filtrate was purified to homogeneity. The distance distribution function p(r) measured by the small angle X-ray scattering technique indicates that the enzyme molecule has a rather unusual tadpole like shape with an isotropic head and a long tail. The maximum length is 18 nm and the largest diameter is 4.4 nm. 

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    Annual Reports on Fermentation Processes", Vol. I l l

    • H. Esterbauer, M. Hayn, G Jungschaffer, E. Taufratzhofer, J. Schurz
    • Enzyme Microb. Technol
    • 1983