Rational enzyme design by reducing the number of hotspots and library size DOI

Zongmin Qin,

Bo Yuan, Ge Qu

et al.

Chemical Communications, Journal Year: 2024, Volume and Issue: 60(76), P. 10451 - 10463

Published: Jan. 1, 2024

Biocatalysts that are eco-friendly, sustainable, and highly specific have great potential for applications in the production of fine chemicals, food, detergents, biofuels, pharmaceuticals, more.

Language: Английский

Development and characterization of a bacterial enzyme cascade reaction system for efficient and stable PET degradation DOI
Chengyong Wang,

Rui Long,

Xiran Lin

et al.

Journal of Hazardous Materials, Journal Year: 2024, Volume and Issue: 472, P. 134480 - 134480

Published: April 29, 2024

Language: Английский

Citations

8
Closed-loop recycling of PET fabric and bottle waste by tandem pre-amorphization and enzymatic hydrolysis DOI
Yu-Hong Cheng,

Yihao Cheng,

Shengcheng Zhou

et al.

Resources Conservation and Recycling, Journal Year: 2024, Volume and Issue: 208, P. 107706 - 107706

Published: May 24, 2024

Language: Английский

Citations

8
Molecular engineering of PETase for efficient PET biodegradation DOI Creative Commons
Tao Wang, Wentao Yang,

Yu-ming Gong

et al.

Ecotoxicology and Environmental Safety, Journal Year: 2024, Volume and Issue: 280, P. 116540 - 116540

Published: June 3, 2024

The widespread utilization of polyethylene terephthalate (PET) has caused a variety environmental and health problems. Compared with traditional thermomechanical or chemical PET cycling, the biodegradation may offer more feasible solution. Though PETase from Ideonalla sakaiensis (IsPETase) displays interesting degrading performance under mild conditions; relatively low thermal stability IsPETase limits its practical application. In this study, enzyme-catalysed degradation was investigated promising mutant HotPETase (HP). On basis, carbohydrate-binding module Bacillus anthracis (BaCBM) fused to C-terminus HP construct (HLCB) for increased degradation. Furthermore, effectively improve accessibility PET-degrading activity, truncated outer membrane hybrid protein (FadL) used expose BaCBM on surface E. coli (BL21with) develop regenerable whole-cell biocatalysts (D-HLCB). Results showed that, among tested small-molecular weight ester compounds (p-nitrophenyl phosphate (pNPP), p-Nitrophenyl acetate (pNPA), 4-Nitrophenyl butyrate (pNPB)), displayed highest hydrolysing activity against pNPP. catalytic (1.94 μM(p-NP)/min) at 50 °C longevity 40 °C. could clearly by increasing optimal reaction temperature improving thermostability. When HLCB degradation, yield monomeric products (255.7 μM) ∼25.5 % greater than that obtained after h HP-catalysed Moreover, D-HLCB-mediated system reached 1.03 mM. catalyst D-HLCB good reusability maintain 54.6 initial nine cycles. Finally, molecular docking simulations were utilized investigate binding mechanism HLCB, which provide theoretical evidence further increase activities PETases through rational design. proposed strategy developed variants show potential achieving complete conditions.

Language: Английский

Citations

8
Engineered polyethylene terephthalate hydrolases: perspectives and limits DOI Creative Commons
Fusako Kawai, Ryo Iizuka, Takeshi Kawabata

et al.

Applied Microbiology and Biotechnology, Journal Year: 2024, Volume and Issue: 108(1)

Published: July 2, 2024

Abstract Polyethylene terephthalate (PET) is a major component of plastic waste. Enzymatic PET hydrolysis the most ecofriendly recycling technology. The biorecycling waste requires complete depolymerization to and ethylene glycol. history enzymatic has revealed two critical issues for industrial PET: industrially available hydrolases pretreatment make it susceptible full hydrolysis. As none wild-type enzymes can satisfy requirements industrialization, various mutational improvements have been performed, through classical technology state-of-the-art computational/machine-learning Recent engineering studies on brought new insight that flexibility substrate-binding groove may improve efficiency while maintaining sufficient thermostability, although previous focused only thermostability above glass transition temperature PET. Industrial scheduled be implemented, using micronized amorphous Next stage must development efficiently degrade crystalline parts expansion target materials, not bottles but also textiles, packages, microplastics. This review discusses current status hydrolases, their potential applications, profespectal goals. Key points • thermophilic, operation below 70 °C Classical approaches are useful Enzyme activity expected future Graphical

Language: Английский

Citations

8
Rational enzyme design by reducing the number of hotspots and library size DOI

Zongmin Qin,

Bo Yuan, Ge Qu

et al.

Chemical Communications, Journal Year: 2024, Volume and Issue: 60(76), P. 10451 - 10463

Published: Jan. 1, 2024

Biocatalysts that are eco-friendly, sustainable, and highly specific have great potential for applications in the production of fine chemicals, food, detergents, biofuels, pharmaceuticals, more.

Language: Английский

Citations

7