Cargando…

Interaction of carbohydrate-binding modules with poly(ethylene terephthalate)

Poly(ethylene terephthalate) (PET) is one of the most widely applied synthetic polymers, but its hydrophobicity is challenging for many industrial applications. Biotechnological modification of PET surface can be achieved by PET hydrolyzing cutinases. In order to increase the adsorption towards thei...

Descripción completa

Detalles Bibliográficos
Autores principales: Weber, Joanna, Petrović, Dušan, Strodel, Birgit, Smits, Sander H. J., Kolkenbrock, Stephan, Leggewie, Christian, Jaeger, Karl-Erich
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6536475/
https://www.ncbi.nlm.nih.gov/pubmed/30993383
http://dx.doi.org/10.1007/s00253-019-09760-9
_version_ 1783421750192635904
author Weber, Joanna
Petrović, Dušan
Strodel, Birgit
Smits, Sander H. J.
Kolkenbrock, Stephan
Leggewie, Christian
Jaeger, Karl-Erich
author_facet Weber, Joanna
Petrović, Dušan
Strodel, Birgit
Smits, Sander H. J.
Kolkenbrock, Stephan
Leggewie, Christian
Jaeger, Karl-Erich
author_sort Weber, Joanna
collection PubMed
description Poly(ethylene terephthalate) (PET) is one of the most widely applied synthetic polymers, but its hydrophobicity is challenging for many industrial applications. Biotechnological modification of PET surface can be achieved by PET hydrolyzing cutinases. In order to increase the adsorption towards their unnatural substrate, the enzymes are fused to carbohydrate-binding modules (CBMs) leading to enhanced activity. In this study, we identified novel PET binding CBMs and characterized the CBM-PET interplay. We developed a semi-quantitative method to detect CBMs bound to PET films. Screening of eight CBMs from diverse families for PET binding revealed one CBM that possesses a high affinity towards PET. Molecular dynamics (MD) simulations of the CBM–PET interface revealed tryptophan residues forming an aromatic triad on the peptide surface. Their interaction with phenyl rings of PET is stabilized by additional hydrogen bonds formed between amino acids close to the aromatic triad. Furthermore, the ratio of hydrophobic to polar contacts at the interface was identified as an important feature determining the strength of PET binding of CBMs. The interaction of CBM tryptophan residues with PET was confirmed experimentally by tryptophan quenching measurements after addition of PET nanoparticles to CBM. Our findings are useful for engineering PET hydrolyzing enzymes and may also find applications in functionalization of PET. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s00253-019-09760-9) contains supplementary material, which is available to authorized users.
format Online
Article
Text
id pubmed-6536475
institution National Center for Biotechnology Information
language English
publishDate 2019
publisher Springer Berlin Heidelberg
record_format MEDLINE/PubMed
spelling pubmed-65364752019-06-12 Interaction of carbohydrate-binding modules with poly(ethylene terephthalate) Weber, Joanna Petrović, Dušan Strodel, Birgit Smits, Sander H. J. Kolkenbrock, Stephan Leggewie, Christian Jaeger, Karl-Erich Appl Microbiol Biotechnol Biotechnologically Relevant Enzymes and Proteins Poly(ethylene terephthalate) (PET) is one of the most widely applied synthetic polymers, but its hydrophobicity is challenging for many industrial applications. Biotechnological modification of PET surface can be achieved by PET hydrolyzing cutinases. In order to increase the adsorption towards their unnatural substrate, the enzymes are fused to carbohydrate-binding modules (CBMs) leading to enhanced activity. In this study, we identified novel PET binding CBMs and characterized the CBM-PET interplay. We developed a semi-quantitative method to detect CBMs bound to PET films. Screening of eight CBMs from diverse families for PET binding revealed one CBM that possesses a high affinity towards PET. Molecular dynamics (MD) simulations of the CBM–PET interface revealed tryptophan residues forming an aromatic triad on the peptide surface. Their interaction with phenyl rings of PET is stabilized by additional hydrogen bonds formed between amino acids close to the aromatic triad. Furthermore, the ratio of hydrophobic to polar contacts at the interface was identified as an important feature determining the strength of PET binding of CBMs. The interaction of CBM tryptophan residues with PET was confirmed experimentally by tryptophan quenching measurements after addition of PET nanoparticles to CBM. Our findings are useful for engineering PET hydrolyzing enzymes and may also find applications in functionalization of PET. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s00253-019-09760-9) contains supplementary material, which is available to authorized users. Springer Berlin Heidelberg 2019-04-16 2019 /pmc/articles/PMC6536475/ /pubmed/30993383 http://dx.doi.org/10.1007/s00253-019-09760-9 Text en © The Author(s) 2019 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Biotechnologically Relevant Enzymes and Proteins
Weber, Joanna
Petrović, Dušan
Strodel, Birgit
Smits, Sander H. J.
Kolkenbrock, Stephan
Leggewie, Christian
Jaeger, Karl-Erich
Interaction of carbohydrate-binding modules with poly(ethylene terephthalate)
title Interaction of carbohydrate-binding modules with poly(ethylene terephthalate)
title_full Interaction of carbohydrate-binding modules with poly(ethylene terephthalate)
title_fullStr Interaction of carbohydrate-binding modules with poly(ethylene terephthalate)
title_full_unstemmed Interaction of carbohydrate-binding modules with poly(ethylene terephthalate)
title_short Interaction of carbohydrate-binding modules with poly(ethylene terephthalate)
title_sort interaction of carbohydrate-binding modules with poly(ethylene terephthalate)
topic Biotechnologically Relevant Enzymes and Proteins
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6536475/
https://www.ncbi.nlm.nih.gov/pubmed/30993383
http://dx.doi.org/10.1007/s00253-019-09760-9
work_keys_str_mv AT weberjoanna interactionofcarbohydratebindingmoduleswithpolyethyleneterephthalate
AT petrovicdusan interactionofcarbohydratebindingmoduleswithpolyethyleneterephthalate
AT strodelbirgit interactionofcarbohydratebindingmoduleswithpolyethyleneterephthalate
AT smitssanderhj interactionofcarbohydratebindingmoduleswithpolyethyleneterephthalate
AT kolkenbrockstephan interactionofcarbohydratebindingmoduleswithpolyethyleneterephthalate
AT leggewiechristian interactionofcarbohydratebindingmoduleswithpolyethyleneterephthalate
AT jaegerkarlerich interactionofcarbohydratebindingmoduleswithpolyethyleneterephthalate