Plastic-Degrading Enzymes from Marine Microorganisms and Their Potential Value in Recycling Technologies DOI Creative Commons
Robert Ruginescu, Cristina Purcărea

Marine Drugs, Journal Year: 2024, Volume and Issue: 22(10), P. 441 - 441

Published: Sept. 26, 2024

Since the 2005 discovery of first enzyme capable depolymerizing polyethylene terephthalate (PET), an aromatic polyester once thought to be enzymatically inert, extensive research has been undertaken identify and engineer new biocatalysts for plastic degradation. This effort was directed toward developing efficient enzymatic recycling technologies that could overcome limitations mechanical chemical methods. These enzymes are versatile molecules obtained from microorganisms living in various environments, including soil, compost, surface seawater, extreme habitats such as hot springs, hydrothermal vents, deep-sea regions, Antarctic seawater. Among plastics, PET polylactic acid (PLA) have primary focus depolymerization research, greatly enhancing our knowledge degrade these specific polymers. They often display unique catalytic properties reflect their particular ecological niches. review explores recent advancements marine-derived can depolymerize synthetic polymers, emphasizing structural functional features influence efficiency catalysts biorecycling processes. Current status future perspectives also discussed, with a on underexplored marine resources.

Language: Английский

Deconstructing PET: Advances in enzyme engineering for sustainable plastic degradation DOI

Jiaxin Yao,

Yao Liu,

Zhenghua Gu

et al.

Chemical Engineering Journal, Journal Year: 2024, Volume and Issue: 497, P. 154183 - 154183

Published: July 21, 2024

Language: Английский

Citations

22

Optimized whole-cell depolymerization of polyethylene terephthalate to monomers using engineered Clostridium thermocellum DOI
Yajun Liu, Fei Yan, Weiliang Dong

et al.

Journal of Hazardous Materials, Journal Year: 2025, Volume and Issue: unknown, P. 137441 - 137441

Published: Jan. 1, 2025

Language: Английский

Citations

3

Protein Engineering for Industrial Biocatalysis: Principles, Approaches, and Lessons from Engineered PETases DOI Open Access
Konstantinos Grigorakis, Christina Ferousi, Evangelos Topakas

et al.

Catalysts, Journal Year: 2025, Volume and Issue: 15(2), P. 147 - 147

Published: Feb. 4, 2025

Protein engineering has emerged as a transformative field in industrial biotechnology, enabling the optimization of enzymes to meet stringent demands for stability, specificity, and efficiency. This review explores principles methodologies protein engineering, emphasizing rational design, directed evolution, semi-rational approaches, recent integration machine learning. These strategies have significantly enhanced enzyme performance, even rendering engineered PETase industrially relevant. Insights from PETases underscore potential tackle environmental challenges, such advancing sustainable plastic recycling, paving way innovative solutions biocatalysis. Future directions point interdisciplinary collaborations emerging learning technologies revolutionize design.

Language: Английский

Citations

3

Tandem Integration of Biological and Electrochemical Catalysis for Efficient Polyester Upcycling under Ambient Conditions DOI
Mengmeng Du, Rui Xue,

Wenfang Yuan

et al.

Nano Letters, Journal Year: 2024, Volume and Issue: 24(31), P. 9768 - 9775

Published: July 26, 2024

Excessive production of waste polyethylene terephthalate (PET) poses an ecological challenge, which necessitates developing technologies to extract the values from end-of-life PET. Upcycling has proven effective in addressing low profitability current recycling strategies, yet existing upcycling operate under energy-intensive conditions. Here we report a cascade strategy steer transformation PET into glycolate overall yield 92.6% ambient The approach involves setting up robust hydrolase with 95.6% depolymerization ethylene glycol (EG) monomer within 12 h, followed by electrochemical process initiated CO-tolerant Pd/Ni(OH)

Language: Английский

Citations

18

Exploring biotechnology for plastic recycling, degradation and upcycling for a sustainable future DOI
Xu Liu, Helen Park, Yannic S. Ackermann

et al.

Biotechnology Advances, Journal Year: 2025, Volume and Issue: unknown, P. 108544 - 108544

Published: Feb. 1, 2025

Language: Английский

Citations

2

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

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

Recycling the recyclers: strategies for the immobilisation of a PET-degrading cutinase DOI Creative Commons
Stefanie Fritzsche, Michael P. Popp,

Lukas Spälter

et al.

Bioprocess and Biosystems Engineering, Journal Year: 2025, Volume and Issue: unknown

Published: Feb. 2, 2025

Abstract Enzymatic degradation of polyethylene terephthalate (PET) represents a sustainable approach to reducing plastic waste and protecting fossil resources. The cost efficiency enzymatic PET processes could be substantially improved by reusing the enzymes. However, conventional immobilisation strategies, such as binding porous carriers, are challenging immobilised enzyme can only interact with macromolecular solid substrate limited extent, thus efficiency. To mitigate this challenge, work compared different strategies PET-degrading cutinase ICCG DAQI . Immobilisation approaches included fixation via linkers synthesis cross-linked aggregates porosities, on stimulus-responsive polymers. highest efficiencies were obtained pH-responsive material Kollicoat ® , where 80% initial activity recovered after immobilisation. Degradation textile fibres cutinase-Kollicoat immobilisate was investigated in batch reactions 1 L-scale. In three consecutive reaction cycles, product yield released terephthalic acid exceeded 97% less than 14 h. Even fifth cycle, 78% maximum achieved same time. An advantage process is efficient pH-dependent recovery reaction, which integrates seamlessly into lowering pH hydrolysis. This integration therefore not simplifies downstream processing, but also provides cost-effective resource-efficient solution for both reuse separation degradation, making it promising industrial application.

Language: Английский

Citations

1

Customization of Ethylene Glycol (EG)‐Induced BmoR‐Based Biosensor for the Directed Evolution of PET Degrading Enzymes DOI Creative Commons
Min Li, Zhenya Chen, Wuyuan Zhang

et al.

Advanced Science, Journal Year: 2025, Volume and Issue: unknown

Published: Feb. 10, 2025

The immense volume of plastic waste poses continuous threats to the ecosystem and human health. Despite substantial efforts enhance catalytic activity, robustness, expression, tolerance plastic-degrading enzymes, lack high-throughput screening (HTS) tools hinders efficient enzyme engineering for industrial applications. Herein, we develop a novel fluorescence-based HTS tool evolving polyethylene terephthalate (PET) degrading enzymes by constructing an engineered BmoR-based biosensor targeting PET breakdown product, ethylene glycol (EG). EG-responsive biosensors, with notably enhanced dynamic range operation range, are customized fluorescence-activated cell sorting (FACS)-assisted transcription factor engineering. ingeniously designed SUMO-MHETase-FastPETase (SMF) chimera successfully addresses functional soluble expression MHETase in Escherichia coli mitigates inhibitory effect mono-(2-hydroxyethyl) terephthalic acid (MHET) intermediate commonly observed PETase alone. obtained SMM3F mutant demonstrates 1.59-fold higher (TPA) production, 1.18-fold decrease Km, 1.29-fold increase Vmax, 1.52-fold kcat/Km, indicating stronger affinity activity toward MHET. Furthermore, crude extract depolymerizes 5 g L-1 bis-(2-hydroxyethyl) (BHET) into TPA completely at 37 °C within 10 h, which is then directedly converted value-added protocatechuic (PCA) (997.16 mg L-1) gallic (GA) (411.69 30 °C, establishing eco-friendly 'PET-BHET-MHET-TPA-PCA-GA' upcycling route. This study provides valuable large-scale MHET hydrolases candidates or metagenomic libraries, propels complete biodegradation waste.

Language: Английский

Citations

1

Enhanced catalytic activity of polyethylene terephthalate hydrolase by structure-guided loop-focused iterative mutagenesis strategy DOI
Wei Lin, Yunxin Zheng, Jiaxing Zhang

et al.

Journal of Hazardous Materials, Journal Year: 2025, Volume and Issue: 490, P. 137837 - 137837

Published: March 5, 2025

Language: Английский

Citations

1