Characterization of a new cutinase from Thermobifida alba for PET-surface hydrolysis

By D. Ribitsch, E. H. Acero, K. Greimel, I. Eiteljoerg, Eva Trotscha, G. Freddi, Helmut Schwab, G. Guebitz. 2012

141 citations recorded by the source corpus.

Subfields: Biomaterials, Health, Toxicology and Mutagenesis, Pollution

View Paper: https://www.semanticscholar.org/paper/145cb0b154939f5ebed30638574b1f23d0dfc5bf

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

1. Gregg T. Beckham
2. D. Ribitsch
3. H. P. Austin
4. Nicholas A. Rorrer
5. Christopher W. Johnson
6. Mark D. Allen
7. E. H. Acero
8. K. Greimel

Citations in the corpus

• Characterization and engineering of a plastic-degrading aromatic polyesterase (2018, background): “Furthermore, we demonstrated that PETase is active on PET of ∼15% crystallinity; while this observation is encouraging, it is envisaged that its performance would need to be enhanced substantially, perhaps via further active-site cleft engineering similar to ongoing work on thermophilic cutinases an”
• A New Esterase from Thermobifida halotolerans Hydrolyses Polyethylene Terephthalate (PET) and Polylactic Acid (PLA) (2012, background): “alba have shown to hydrolyze PET-films [27,42].”