Enhanced Adsorption and Enzymatic Hydrolysis of Polyethylene Terephthalate by Cutinase with an N‑Terminal Hydrophobic Tether

Enhanced Adsorption and Enzymatic Hydrolysis of Polyethylene Terephthalate by Cutinase with an N‑Terminal Hydrophobic Tether

The environmental challenges presented by plastic waste, particularly poly(ethylene terephthalate) (PET), necessitate innovative biodegradation strategies. The cutinase from Thermobifida cellulosilytica, Thc_Cut1 (Cut), was site-specifically conjugated with alkyl tethers of varying lengths (C<sub...

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Bibliographic Details
Main Author: Md Sadikur Rahman Shuvo (22374895) (author)
Other Authors: Doris Ribitsch (1462945) (author), Georg M. Gübitz (22374898) (author), Shuichiro Seno (1950016) (author), Takayuki Uchihashi (691641) (author), Akira Onoda (1470163) (author)
Published: 2025
Subjects:
Biochemistry
Cell Biology
Biotechnology
Infectious Diseases
Plant Biology
Space Science
Environmental Sciences not elsewhere classified
Chemical Sciences not elsewhere classified
scanning electron microscopy
ray photoelectron spectroscopy
environmental challenges presented
69 %, respectively
unconjugated cutinases revealed
enzyme kinetic parameters
pet surfaces compared
pet surface following
increased enzyme adsorption
pet hydrolysis efficiency
pet surface
enzyme ’
enzyme treatment
pet film
improving hydrolysis
enzymatic hydrolysis
stable adsorption
slower adsorption
enhanced adsorption
unconjugated cutinase
varying lengths
thermobifida cellulosilytica
terminus strengthens
terephthalic acid
significant improvement
results suggest
polyethylene terephthalate
plastic waste
particularly poly
minimal impact
higher affinity
h </
ethylene terephthalate
enhanced erosion
enhance affinity
cut ),
catalytic activity
alkyl tethers
alkyl tether
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