4.5 Article

Efficient depolymerization of polyethylene terephthalate (PET) and polyethylene furanoate by engineered PET hydrolase Cut190

Related references

Note: Only part of the references are listed.
Article Chemistry, Physical

Substrate-Binding Mode of a Thermophilic PET Hydrolase and Engineering the Enzyme to Enhance the Hydrolytic Efficacy

Wei Zeng et al.

Summary: Polyethylene terephthalate (PET) is a widely produced plastic with high accumulation of PET wastes posing a serious threat to the ecosystem. The application of PET hydrolytic enzymes to manage PET pollution requires more effective enzymes. A thermostable cutinase called ICCG has shown to be the most effective PET hydrolase reported so far. The crystal structure of ICCG in complex with PET analogue provides insights into the enzyme-substrate interaction network and structure-based engineering has generated variants with improved efficacy and stability. These findings are valuable for understanding the mechanism of thermostable PET hydrolytic enzymes and developing PET biodegradation platforms.

ACS CATALYSIS (2022)

Article Chemistry, Multidisciplinary

Low Carbon Footprint Recycling of Post-Consumer PET Plastic with a Metagenomic Polyester Hydrolase

Christian Sonnendecker et al.

Summary: Enzyme-based hydrolysis is a promising strategy for sustainable recycling of plastics. A study found that the enzyme PHL7 can completely degrade plastics and the products can be used to synthesize new plastics.

CHEMSUSCHEM (2022)

Article Chemistry, Multidisciplinary

Discovery and Genetic Code Expansion of a Polyethylene Terephthalate (PET) Hydrolase from the Human Saliva Metagenome for the Degradation and Bio-Functionalization of PET

Bhumrapee Eiamthong et al.

Summary: We report the discovery of a new PET hydrolase, named MG8, from the human saliva metagenome. MG8 exhibits robust PET degradation activities under different conditions and outperforms other hydrolases in degrading PET. Furthermore, we genetically modified MG8 to serve as a covalent binder for PET functionalization, enabling the attachment of protein cargos to PET and other polyester plastics.

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2022)

Article Multidisciplinary Sciences

Machine learning-aided engineering of hydrolases for PET depolymerization

Hongyuan Lu et al.

Summary: Plastic waste is an ecological challenge, and enzymatic degradation offers a potentially green and scalable route for plastic recycling. Engineered PETase shows superior activity in hydrolyzing postconsumer PET, and a closed-loop recycling process is demonstrated.

NATURE (2022)

Article Chemistry, Physical

Mechanism-Based Design of Efficient PET Hydrolases

Ren Wei et al.

Summary: Polyethylene terephthalate (PET) is a widely used synthetic polyester in textile fibers and packaging materials, which contributes significantly to global solid waste and environmental plastic pollution. Enzymatic PET recycling and upcycling have emerged as potential solutions, but there are limitations such as unbalanced enzyme-substrate interactions, limited thermostability, low catalytic efficiency at high temperatures, and inhibition by degradation intermediates. Protein engineering has been successful in addressing these limitations and can be applied to other mass-produced polymer types for biotechnological waste disposal.

ACS CATALYSIS (2022)

Article Engineering, Environmental

Directional-path modification strategy enhances PET hydrolase catalysis of plastic degradation

Xiao-Qian Chen et al.

Summary: PET degradation efficiency can be significantly enhanced by the novel DPM strategy proposed in this study. Molecular simulations revealed the mechanism behind the improved degradation and demonstrated the effectiveness and universality of the DPM strategy in various enzymes.

JOURNAL OF HAZARDOUS MATERIALS (2022)

Article Biochemical Research Methods

Influence of substrate crystallinity and glass transition temperature on enzymatic degradation of polyethylene terephthalate (PET)

Thore Bach Thomsen et al.

Summary: This work investigates the importance of the degree of crystallinity and glass transition temperature of PET on enzymatic degradation at elevated temperatures. The results show that the crystallinity affects the enzymatic product release rate, and different enzymes exhibit different activities at varying degrees of crystallinity. In addition, thermal annealing and water soaking have an impact on the properties of PET. These findings contribute to a better understanding of enzymatic PET degradation and the development of PET upcycling processes.

NEW BIOTECHNOLOGY (2022)

Article Chemistry, Physical

Multiple Substrate Binding Mode-Guided Engineering of a Thermophilic PET Hydrolase

Lara Pfaff et al.

Summary: Thermophilic polyester hydrolases (PES-H) play a crucial role in the biocatalytic recycling of synthetic polyester polyethylene terephthalate (PET). By studying the crystal structures of two enzymes derived from metagenomes, researchers gained insights into the mechanism of enzymatic PET hydrolysis. Mutations in key residues resulted in improved hydrolytic activity of certain variants, making them potential candidates for industrial plastic recycling processes.

ACS CATALYSIS (2022)

Article Chemistry, Multidisciplinary

Particle Size Reduction of Poly(ethylene terephthalate) Increases the Rate of Enzymatic Depolymerization But Does Not Increase the Overall Conversion Extent

Richard K. Brizendine et al.

Summary: Enzymatic depolymerization of PET is a potential method for PET recycling, but extensive thermomechanical preprocessing is often conducted. In this study, the effect of PET particle size and crystallinity on the performance of a specific enzyme was investigated using different types of PET. The results show that particle size reduction can increase the reaction rate for high-crystallinity PET, but has little effect on the overall conversion extent. Amorphization of PET is necessary for enzymatic PET recycling, while particle size reduction may not be required.

ACS SUSTAINABLE CHEMISTRY & ENGINEERING (2022)

Article Chemistry, Physical

Directed evolution of an efficient and thermostable PET depolymerase

Elizabeth L. Bell et al.

Summary: The recent discovery of IsPETase, a hydrolytic enzyme that can degrade polyethylene terephthalate (PET), has sparked interest in using biocatalytic approaches to recycle plastics. In this study, we describe an automated, high-throughput directed evolution platform for engineering polymer degrading enzymes. By applying catalytic activity under elevated temperatures, a thermostable IsPETase variant (HotPETase) was successfully engineered to operate at the industrial processing temperature of PET. This HotPETase enzyme showed improved efficiency in degrading PET compared to previously reported enzymes and could selectively breakdown the PET component of multi-materials.

NATURE CATALYSIS (2022)

Article Chemistry, Multidisciplinary

Sabatier Principle for Rationalizing Enzymatic Hydrolysis of a Synthetic Polyester

Jenny Arnling Baath et al.

Summary: Investigated the kinetics of two PET hydrolases at different concentrations of CTAB and found that CTAB consistently lowered the strength of enzyme-PET interactions. The effect of CTAB on enzymatic turnover was biphasic, with initial promotion and subsequent suppression. The correlation with maximal turnover at an intermediate binding strength was in accordance with the Sabatier principle. Suggested that future discovery efforts should consider enzymes with weakened substrate binding due to their limiting effect on catalytic performance.

JACS AU (2022)

Article Biochemistry & Molecular Biology

Multiple structural states of Ca2+-regulated PET hydrolase, Cut190, and its correlation with activity and stability

Akane Senga et al.

Summary: The catalytic activity and stability of the enzyme Cut190, and its mutant Cut190*, are regulated by Ca2+ binding. Crystal structure studies revealed multiple forms of Cut190* and its mutants, and the deletion of C-terminal residues increased thermal stability while retaining activity. This increased stability can be utilized for protein engineering of Cut190 for PET depolymerization.

JOURNAL OF BIOCHEMISTRY (2021)

Article Biochemistry & Molecular Biology

Structural basis of mutants of PET-degrading enzyme from Saccharomonospora viridis AHK190 with high activity and thermal stability

Miho Emori et al.

Summary: The study demonstrated that Cut190*SS increased thermal stability while maintaining enzymatic function, attributed to the formation of a disulfide bond by Cys250 and Cys296. Results indicated that although the metal-binding properties of Cut190*SS series differed, the enzyme retained its ability to utilize Ca2+ to accelerate conformational change, thereby preserving its functionality.

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS (2021)

Article Chemistry, Physical

Computational Redesign of a PETase for Plastic Biodegradation under Ambient Condition by the GRAPE Strategy

Yinglu Cui et al.

Summary: This study successfully improved the robustness of PETase through a computational strategy, resulting in the redesign of a variant DuraPETase with significantly elevated melting temperature and enhanced degradation of PET films, as well as complete biodegradation of microplastics at mild temperatures. The design strategy presents opportunities for handling uncollectable PET waste and converting resulting monomers into high-value molecules.

ACS CATALYSIS (2021)

Article Biotechnology & Applied Microbiology

Secretory expression in Bacillus subtilis and biochemical characterization of a highly thermostable polyethylene terephthalate hydrolase from bacterium HR29

Xingxiang Xi et al.

Summary: The environmental threat of plastic waste disposal has been a major concern, and recycling PET waste into reusable materials has become a solution. This study introduced a highly efficient PETase, BhrPETase, with superior hydrolyzing activity towards amorphous PET and remarkable thermostability, making it a promising candidate for PET recycling and bioremediation applications.

ENZYME AND MICROBIAL TECHNOLOGY (2021)

Article Chemistry, Physical

Highly Crystalline Post-Consumer PET Waste Hydrolysis by Surface Displayed PETase Using a Bacterial Whole-Cell Biocatalyst

David Gercke et al.

Summary: A new bacterial whole-cell biocatalyst was constructed for enzymatic degradation of PET waste, utilizing surface display of PETase and environmentally benign rhamnolipids. This approach led to a more efficient PET degradation, outperforming free PETase by a factor of 16.

CHEMCATCHEM (2021)

Review Chemistry, Multidisciplinary

Emerging Strategies in Polyethylene Terephthalate Hydrolase Research for Biorecycling

Fusako Kawai

Summary: Research on PET hydrolyzing enzymes aims to increase thermostability for higher activity, as well as to pretreat waste PET for biodegradability. Improving enzyme thermostabilities through gene mutation, host expression, and modifications, as well as processing waste PET into more readily biodegradable forms, are crucial for achieving PET biorecycling.

CHEMSUSCHEM (2021)

Article Chemistry, Physical

Techno-economic, life-cycle, and socioeconomic impact analysis of enzymatic recycling of poly(ethylene terephthalate)

Avantika Singh et al.

Summary: Esterases play a crucial role in enzymatic PET recycling, enabling efficient depolymerization to TPA and ethylene glycol, reducing energy consumption and greenhouse gas emissions, and generating more socio-economic benefits.

JOULE (2021)

Article Chemistry, Multidisciplinary

Current State and Perspectives Related to the Polyethylene Terephthalate Hydrolases Available for Biorecycling

Fusako Kawai et al.

ACS SUSTAINABLE CHEMISTRY & ENGINEERING (2020)

Article Multidisciplinary Sciences

An engineered PET depolymerase to break down and recycle plastic bottles

V. Tournier et al.

NATURE (2020)

Article Chemistry, Physical

Cryo vs Thermo: Duality of Ethylene Glycol on the Stability of Proteins

K. Tejaswi Naidu et al.

JOURNAL OF PHYSICAL CHEMISTRY B (2020)

Article Thermodynamics

Folding thermodynamics of PET-hydrolyzing enzyme Cut190 depending on Ca2+ concentration

Satomi Inaba et al.

JOURNAL OF THERMAL ANALYSIS AND CALORIMETRY (2019)

Review Biotechnology & Applied Microbiology

Current knowledge on enzymatic PET degradation and its possible application to waste stream management and other fields

Fusako Kawai et al.

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY (2019)

Article Multidisciplinary Sciences

Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrate

Gottfried J. Palm et al.

NATURE COMMUNICATIONS (2019)

Article Biotechnology & Applied Microbiology

Enzymatic hydrolysis of PET: functional roles of three Ca2+ ions bound to a cutinase-like enzyme, Cut190*, and its engineering for improved activity

Masayuki Oda et al.

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY (2018)

Article Biotechnology & Applied Microbiology

Mutational analysis of cutinase-like enzyme, Cut190, based on the 3D docking structure with model compounds of polyethylene terephthalate

Takeshi Kawabata et al.

JOURNAL OF BIOSCIENCE AND BIOENGINEERING (2017)

Article Biochemistry & Molecular Biology

Enzymatic recovery of polyester building blocks from polymer blends

Caroline Gamerith et al.

PROCESS BIOCHEMISTRY (2017)

Article Multidisciplinary Sciences

Production, use, and fate of all plastics ever made

Roland Geyer et al.

SCIENCE ADVANCES (2017)

Article Biotechnology & Applied Microbiology

Engineered Bacterial Polyester Hydrolases Efficiently Degrade Polyethylene Terephthalate Due to Relieved Product Inhibition

Ren Wei et al.

BIOTECHNOLOGY AND BIOENGINEERING (2016)

Review Biotechnology & Applied Microbiology

Enzymatic hydrolysis of poly(ethylene furanoate)

Alessandro Pellis et al.

JOURNAL OF BIOTECHNOLOGY (2016)

Article Multidisciplinary Sciences

A bacterium that degrades and assimilates poly(ethylene terephthalate)

Shosuke Yoshida et al.

SCIENCE (2016)

Article Biotechnology & Applied Microbiology

Comparison of genetic structures and biochemical properties of tandem cutinase-type polyesterases from Thermobifida alba AHK119

Uschara Thumarat et al.

JOURNAL OF BIOSCIENCE AND BIOENGINEERING (2015)

Article Biotechnology & Applied Microbiology

Structural basis for the Ca2+-enhanced thermostability and activity of PET-degrading cutinase-like enzyme from Saccharomonospora viridis AHK190

Takuya Miyakawa et al.

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY (2015)

Article Biotechnology & Applied Microbiology

A novel Ca2+-activated, thermostabilized polyesterase capable of hydrolyzing polyethylene terephthalate from Saccharomonospora viridis AHK190

Fusako Kawai et al.

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY (2014)

Article Biochemistry & Molecular Biology

Crystal Structure and Thermodynamic and Kinetic Stability of Metagenome-Derived LC-Cutinase

Sintawee Sulaiman et al.

BIOCHEMISTRY (2014)

Review Biotechnology & Applied Microbiology

Biochemistry of microbial polyvinyl alcohol degradation

Fusako Kawai et al.

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY (2009)

Article Biochemistry & Molecular Biology

Mechanisms of Protein Stabilization and Prevention of Protein Aggregation by Glycerol

Vincent Vagenende et al.

BIOCHEMISTRY (2009)

Article Polymer Science

Cutinase-Catalyzed Hydrolysis of Poly(ethylene terephthalate)

Asa M. Ronkvist et al.

MACROMOLECULES (2009)

Article Biochemistry & Molecular Biology

Biological degradation of synthetic polyesters - Enzymes as potential catalysts for polyester recycling

Rolf-Joachim Mueller

PROCESS BIOCHEMISTRY (2006)

Article Polymer Science

Enzymatic degradation of poly(ethylene terephthalate):: Rapid hydrolyse using a hydrolase from T-fusca

RJ Müller et al.

MACROMOLECULAR RAPID COMMUNICATIONS (2005)