Fusion of Hydrophobic Anchor Peptides Promotes the Hydrolytic Activity of PETase but not the Extent of PET Depolymerization DOI
Yongjie Wang,

Ekram Akram,

Yujing Ding

et al.

ChemCatChem, Journal Year: 2024, Volume and Issue: unknown

Published: Oct. 28, 2024

Abstract Enzymatic recycling of polyethylene terephthalate (PET) has attracted significant attention in recent years. While the fusion anchor peptides to PET hydrolases is believed enhance hydrolytic activity, a quantitative analysis yet lacking. Here, we construct four enzymes by fusing (including hydrophobic LCI, LCIM1 and TA2, hydrophilic EK4) C terminus HotPETase, one most active for high‐crystallinity (HC‐PET). Single‐molecule force spectroscopy (SMFS) demonstrates that promote adhesive interactions between surface. This also validated adsorption kinetics isotherms, saturated capacity remains unaltered compared HotPETase. At low substrate loadings, apparent activity these positively related hydrophobicity peptides. Among them, HotPETase‐LCI stands out as effective enzyme HC‐PET degradation, demonstrating 1.5‐fold increase activity. high advantages with diminish. We conclude only facilitate rates reactions but have little effect on final conversion extent.

Language: Английский

Efficient Bioprocess for Mixed PET Waste Depolymerization Using Crude Cutinase DOI Open Access
Virender Kumar, Reinhard Wimmer, Cristiano Varrone

et al.

Polymers, Journal Year: 2025, Volume and Issue: 17(6), P. 763 - 763

Published: March 14, 2025

In recent years, several plastic-degrading enzymes with efficient depolymerization abilities for PET have been reported. Here, we report a bioprocess mixed waste using crude extracellularly expressed in E. coli. The enzymes, namely FastPETase, LCC, and LCCICCG, were screened to depolymerize amorphous powder films of different sizes crystallinity. LCCICCG achieved approximately 25, 34, 70% depolymerization, respectively, when applied 13 g L−1 film, powder, or optimized enzyme conditions without any pH control. yield terephthalic acid the hydrolytic process was maximum followed by LCC FastPETase. Finally, extracellular LCCICCG-producing coli cells cultivated minimal media supplemented 0.1% ammonium chloride 1% glycerol as nitrogen carbon sources bioreactor final protein content specific activity 119 ± 5 mg 1232 18 U mg−1, respectively. Nearly complete 23.8 post-consumer 50 h supernatant, purification, at 62 °C. A thus developed 100 trays bottle (MW1 MW2), reaching 78% 50% °C loading 2.32 g−1 60 h. results demonstrate an easy strategy that could be exploited large-scale facilities plastic treatment.

Language: Английский

Citations

0
State-of-the-art advances in biotechnology for polyethylene terephthalate bio-depolymerization DOI Creative Commons
Yajun Liu, Jie Zhou, Yanwei Li

et al.

Green Carbon, Journal Year: 2025, Volume and Issue: unknown

Published: March 1, 2025

Language: Английский

Citations

0
Interfacial catalysis in enzymatic PET plastic depolymerization DOI
Jie Zhou, Zhongli Cui, Ren Wei

et al.

Trends in Chemistry, Journal Year: 2025, Volume and Issue: unknown

Published: March 1, 2025

Language: Английский

Citations

0
Influence of Wobbling Tryptophan and Mutations on PET Degradation Explored by QM/MM Free Energy Calculations DOI Creative Commons
Anna Jäckering, Marc W. van der Kamp, Birgit Strodel

et al.

Journal of Chemical Information and Modeling, Journal Year: 2024, Volume and Issue: unknown

Published: Sept. 29, 2024

Plastic-degrading enzymes, particularly poly(ethylene terephthalate) (PET) hydrolases, have garnered significant attention in recent years as potential eco-friendly solutions for recycling plastic waste. However, understanding of their PET-degrading activity and influencing factors remains incomplete, impeding the development uniform approaches enhancing PET hydrolases industrial applications. A key aspect hydrolase engineering is optimizing PET-hydrolysis reaction by lowering associated free energy barrier. inconsistent findings complicated these efforts. Therefore, our goal to elucidate various aspects enzymatic degradation means quantum mechanics/molecular mechanics (QM/MM) simulations analysis, focusing on initial step, acylation, two thermophilic LCC PES-H1, along with highly active variants,

Language: Английский

Citations

2
Fusion of Hydrophobic Anchor Peptides Promotes the Hydrolytic Activity of PETase but not the Extent of PET Depolymerization DOI
Yongjie Wang,

Ekram Akram,

Yujing Ding

et al.

ChemCatChem, Journal Year: 2024, Volume and Issue: unknown

Published: Oct. 28, 2024

Abstract Enzymatic recycling of polyethylene terephthalate (PET) has attracted significant attention in recent years. While the fusion anchor peptides to PET hydrolases is believed enhance hydrolytic activity, a quantitative analysis yet lacking. Here, we construct four enzymes by fusing (including hydrophobic LCI, LCIM1 and TA2, hydrophilic EK4) C terminus HotPETase, one most active for high‐crystallinity (HC‐PET). Single‐molecule force spectroscopy (SMFS) demonstrates that promote adhesive interactions between surface. This also validated adsorption kinetics isotherms, saturated capacity remains unaltered compared HotPETase. At low substrate loadings, apparent activity these positively related hydrophobicity peptides. Among them, HotPETase‐LCI stands out as effective enzyme HC‐PET degradation, demonstrating 1.5‐fold increase activity. high advantages with diminish. We conclude only facilitate rates reactions but have little effect on final conversion extent.

Language: Английский

Citations

1