- AutorIn
- Johannes Then
- Ren Wei
- Thorsten Oeser
- André Gerdts
- Juliane Schmidt
- Markus Barth
- Wolfgang Zimmermann
- Titel
- A disulfide bridge in the calcium binding site of a polyester hydrolase increases its thermal stability and activity against polyethylene terephthalate
- Zitierfähige Url:
- https://nbn-resolving.org/urn:nbn:de:bsz:15-qucosa-205582
- Quellenangabe
- FEBS Open Bio 6 (2016) 425–432 doi: 10.1002/2211-5463.12053
- Erstveröffentlichung
- 2016
- Abstract (EN)
- Elevated reaction temperatures are crucial for the efficient enzymatic degradation of polyethylene terephthalate (PET). A disulfide bridge was introduced to the polyester hydrolase TfCut2 to substitute its calcium binding site. The melting point of the resulting variant increased to 94.7°C (wild-type TfCut2: 69.8 °C) and its half-inactivation temperature to 84.6 °C (TfCut2: 67.3 °C). The variant D204C-E253C-D174R obtained by introducing further mutations at vicinal residues showed a temperature optimum between 75 and 80 °C compared to 65 and 70 °C of the wild-type enzyme. The variant caused a weight loss of PET films of 25.0 +/- 0.8% (TfCut2: 0.3 +/-0.1%) at 70 °C after a reaction time of 48 h. The results demonstrate that a highly efficient and calcium-independent thermostable polyester hydrolase can be obtained by replacing its calcium binding site with a disulfide bridge.
- Andere Ausgabe
- Link zur Originalpublikation in der Zeitschrift FEBS Open Bio
Link: http://dx.doi.org/10.1002/2211-5463.12053 - Freie Schlagwörter (DE)
- Biokatalyse, Kalzium, Disulfidbrücke, Polyethylenterephthalat, Protein-Engineering, Proteinstabilität
- Freie Schlagwörter (EN)
- biocatalysis, calcium, disulfide bridge, polyethylene terephthalate, protein engineering, protein stability
- Klassifikation (DDC)
- 540
- 570
- Herausgeber (Institution)
- Universität Leipzig
- Verlag
- Elsevier, Cambridge
- URN Qucosa
- urn:nbn:de:bsz:15-qucosa-205582
- Veröffentlichungsdatum Qucosa
- 23.06.2016
- Dokumenttyp
- Artikel
- Sprache des Dokumentes
- Englisch