This title appears in the Scientific Report :
2019
Please use the identifier:
http://dx.doi.org/10.1007/s00253-019-09760-9 in citations.
Please use the identifier: http://hdl.handle.net/2128/23884 in citations.
Interaction of carbohydrate-binding modules with poly(ethylene terephthalate)
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...
Saved in:
Personal Name(s): | Weber, Joanna |
---|---|
Petrović, Dušan / Strodel, Birgit / Smits, Sander H. J. / Kolkenbrock, Stephan / Leggewie, Christian / Jaeger, Karl-Erich (Corresponding author) | |
Contributing Institute: |
Institut für Molekulare Enzymtechnologie (HHUD); IMET Strukturbiochemie; ICS-6 |
Published in: | Applied microbiology and biotechnology, 103 (2019) 12, S. 4801 - 4812 |
Imprint: |
New York
Springer
2019
|
PubMed ID: |
30993383 |
DOI: |
10.1007/s00253-019-09760-9 |
Document Type: |
Journal Article |
Research Program: |
Functional Macromolecules and Complexes |
Link: |
OpenAccess OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://hdl.handle.net/2128/23884 in citations.
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. |