Applied Microbiology and Biotechnology

, Volume 98, Issue 18, pp 7815–7823 | Cite as

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

Biotechnologically relevant enzymes and proteins

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.

Keywords

Cutinase Crystal structure Thermostability PET degradation PET modification 

Notes

Conflict of interest

The authors declare that they have no conflict of interest.

Supplementary material

253_2014_5672_MOESM1_ESM.pdf (517 kb)
ESM 1(PDF 517 kb)

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Copyright information

© Springer-Verlag Berlin Heidelberg 2014

Authors and Affiliations

  1. 1.Institut für Bioanalytische Chemie, Fakultät für Chemie und MineralogieUniversität LeipzigLeipzigGermany
  2. 2.Institut für Biochemie, Fakultät für Biowissenschaften, Pharmazie und PsychologieUniversität LeipzigLeipzigGermany
  3. 3.York Structural Biology Laboratory, Department of ChemistryThe University of YorkYorkUK

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