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Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca

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Abstract

Bacterial cutinases are promising catalysts for the modification and degradation of the widely used plastic polyethylene terephthalate (PET). The improvement of the enzyme for industrial purposes is limited due to the lack of structural information for cutinases of bacterial origin. We have crystallized and structurally characterized a cutinase from Thermobifida fusca KW3 (TfCut2) in free as well as in inhibitor-bound form. Together with our analysis of the thermal stability and modelling studies, we suggest possible reasons for the outstanding thermostability in comparison to the less thermostable homolog from Thermobifida alba AHK119 and propose a model for the binding of the enzyme towards its polymeric substrate. The TfCut2 structure is the basis for the rational design of catalytically more efficient enzyme variants for the hydrolysis of PET and other synthetic polyesters.

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  1. Christian Roth

    Present address: York Structural Biology Laboratory, Department of Chemistry, The University of York, York, YO10 5DD, UK

Authors and Affiliations

  1. Institut für Bioanalytische Chemie, Fakultät für Chemie und Mineralogie, Universität Leipzig, Leipzig, Germany

    Christian Roth & Norbert Sträter

  2. Institut für Biochemie, Fakultät für Biowissenschaften, Pharmazie und Psychologie, Universität Leipzig, Leipzig, Germany

    Ren Wei, Thorsten Oeser, Johannes Then, Christina Föllner & Wolfgang Zimmermann

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  1. Christian Roth
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Correspondence to Christian Roth, Wolfgang Zimmermann or Norbert Sträter.

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Roth, C., Wei, R., Oeser, T. et al. Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca . Appl Microbiol Biotechnol 98, 7815–7823 (2014). https://doi.org/10.1007/s00253-014-5672-0

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