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

Roth, C., Wei, R., Oeser, T., Then, J., Föllner, C., Zimmermann, W., et al. (2014). Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca. Applied Microbiology and Biotechnology, 98(18), 7815-7823. doi:10.1007/s00253-014-5672-0.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0000-24DA-2 Version Permalink: http://hdl.handle.net/21.11116/0000-0000-24DB-1
Genre: Journal Article

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 Creators:
Roth, Christian1, Author              
Wei, Ren, Author
Oeser, Thorsten, Author
Then, Johannes, Author
Föllner, Christina, Author
Zimmermann, Wolfgang, Author
Sträter, Norbert, Author
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1External Organizations, ou_persistent22              

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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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 Dates: 2014-09
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: -
 Identifiers: DOI: 10.1007/s00253-014-5672-0
BibTex Citekey: Roth2014
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Title: Applied Microbiology and Biotechnology
Source Genre: Journal
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Publ. Info: Heidelberg : Springer-Verlag
Pages: - Volume / Issue: 98 (18) Sequence Number: - Start / End Page: 7815 - 7823 Identifier: ISSN: 0175-7598