Enzymatic Degradation of Poly(ethylene terephthalate): Rapid Hydrolyse using a Hydrolase from T. fusca
By R. Müller, H. Schrader, Jörn Profe, Karolin Dresler, W. Deckwer. 2005
539 citations recorded by the source corpus.
Subfields: Biomaterials, Industrial and Manufacturing Engineering, Pollution
View Paper: https://www.semanticscholar.org/paper/26bb4d287352f6be042a364add1945a6693fa7d2
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Citations in the corpus
- Biological degradation of synthetic polyesters—Enzymes as potential catalysts for polyester recycling (2006, background): “fusca (TfH) to an extent and at a rate which may open the door for a future biological recycling of such polyesters [22].”
- Characterization of a new cutinase from Thermobifida alba for PET-surface hydrolysis (2012, background): “Thermobifi da cutinases have been reported to be superior to fungal cutinases in terms of temperature optima, which not only allows higher reaction rates but also increases mobilty of the PET chains and thus accessibility of the enzyme to the substrate (M ü ller et al. 2005).”
- Microbial and Enzymatic Degradation of Synthetic Plastics (2020, background): “…nitrogen and energy source for growth, e.g., P. aeruginosa (Kay et al., 1991), Corynebacterium sp. (Kay et al., 1991), Comamonas acidovorans (Nakajima-Kambe et al., 1995), Pseudomonas fluorescens (Howard and Blake, 1998), Acinetobacter calcoaceticus (El-Sayed et al., 1996), and Bacillus…”
- Enhanced Poly(ethylene terephthalate) Hydrolase Activity by Protein Engineering (2018, methodology): “After centrifuging at 12 000 r min 1 for 1 min, 200 lL of supernatant was pipetted into a 96 well plate, and the absorbance at 240 nm was measured with a microplate reader [15].”
- 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”