A Novel Polyester Hydrolase From the Marine Bacterium Pseudomonas aestusnigri – Structural and Functional Insights DOI Creative Commons
Alexander Bollinger, Stephan Thies, Esther Knieps‐Grünhagen

et al.

Frontiers in Microbiology, Journal Year: 2020, Volume and Issue: 11

Published: Feb. 12, 2020

Biodegradation of synthetic polymers, in particular polyethylene terephthalate (PET), is great importance, since environmental pollution with PET and other plastics has become a severe global problem. Here, we report on the polyester degrading ability novel carboxylic ester hydrolase identified genome marine hydrocarbonoclastic bacterium Pseudomonas aestusnigri VGXO14 T . The enzyme, designated PE-H, belongs to type IIa family hydrolytic enzymes as indicated by amino acid sequence homology. It was produced Escherichia coli, purified its crystal structure solved at 1.09 Å resolution representing first enzyme. shows typical α/β-hydrolase fold high structural homology known hydrolases. hydrolysis detected 30°C amorphous film (PETa), but not from commercial bottle (PETb). A rational mutagenesis study improve potential PE-H yielded variant (Y250S) which showed improved activity, ultimately also allowing PETb. this 1.35 allowed rationalize improvement enzymatic activity. oligomer binding model proposed molecular docking computations. Our results indicate significant P. for degradation.

Language: Английский

Computational Redesign of a PETase for Plastic Biodegradation under Ambient Condition by the GRAPE Strategy DOI
Yinglu Cui, Yanchun Chen,

Xinyue Liu

et al.

ACS Catalysis, Journal Year: 2021, Volume and Issue: 11(3), P. 1340 - 1350

Published: Jan. 13, 2021

Nature has provided a fantastic array of enzymes that are responsible for essential biochemical functions but not usually suitable technological applications. Not content with the natural repertoire, protein engineering holds promise to extend applications improved tailored properties. However, robust proteins remains difficult task since positive mutation library may cooperate reach target function in most cases owing ubiquity epistatic effects. The main demand lies identifying an efficient path accumulated mutations. Herein, we devised computational strategy (greedy engineering, GRAPE) improve robustness PETase from Ideonella sakaiensis. A systematic clustering analysis combined greedy accumulation beneficial mutations computationally derived enabled redesign variant, DuraPETase, which exhibits apparent melting temperature is drastically elevated by 31 °C and strikingly enhanced degradation toward semicrystalline poly(ethylene terephthalate) (PET) films (30%) at mild temperatures (over 300-fold). Complete biodegradation 2 g/L microplastics water-soluble products under conditions also achieved, opening up opportunities steer biological uncollectable PET waste further conversion resulting monomers high-value molecules. crystal structure revealed individual match design model. Concurrently, synergistic effects captured, while interactions alleviated during process. We anticipate our will provide broadly applicable global optimization enzyme performance.

Language: Английский

Citations

437
Polyethylene terephthalate (PET) in the packaging industry DOI
Roberto Nisticò

Polymer Testing, Journal Year: 2020, Volume and Issue: 90, P. 106707 - 106707

Published: July 28, 2020

Language: Английский

Citations

407
Characterization and engineering of a two-enzyme system for plastics depolymerization DOI Creative Commons
Brandon C. Knott, Erika Erickson, Mark D. Allen

et al.

Proceedings of the National Academy of Sciences, Journal Year: 2020, Volume and Issue: 117(41), P. 25476 - 25485

Published: Sept. 28, 2020

Significance Deconstruction of recalcitrant polymers, such as cellulose or chitin, is accomplished in nature by synergistic enzyme cocktails that evolved over millions years. In these systems, soluble dimeric oligomeric intermediates are typically released via interfacial biocatalysis, and additional enzymes often process the into monomers for microbial uptake. The recent discovery a two-enzyme system polyethylene terephthalate (PET) deconstruction, which employs one to convert polymer another produce constituent PET (MHETase), suggests may be evolving similar deconstruction strategies synthetic plastics. This study on characterization MHETase synergy depolymerization inform cocktail-based plastics upcycling.

Language: Английский

Citations

398
Catalytic processing of plastic waste on the rise DOI Creative Commons
Antonio J. Martín, Cecilia Mondelli, Shibashish D. Jaydev

et al.

Chem, Journal Year: 2021, Volume and Issue: 7(6), P. 1487 - 1533

Published: Jan. 10, 2021

Language: Английский

Citations

397
Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrate DOI Creative Commons
Gottfried J. Palm, Lukas Reisky, Dominique Böttcher

et al.

Nature Communications, Journal Year: 2019, Volume and Issue: 10(1)

Published: April 12, 2019

Abstract The extreme durability of polyethylene terephthalate (PET) debris has rendered it a long-term environmental burden. At the same time, current recycling efforts still lack sustainability. Two recently discovered bacterial enzymes that specifically degrade PET represent promising solution. First, Ideonella sakaiensis PETase, structurally well-characterized consensus α/β-hydrolase fold enzyme, converts to mono-(2-hydroxyethyl) (MHET). MHETase, second key hydrolyzes MHET educts and ethylene glycol. Here, we report crystal structures active ligand-free MHETase bound nonhydrolyzable analog. which is reminiscent feruloyl esterases, possesses classic domain lid conferring substrate specificity. In light structure-based mapping site, activity assays, mutagenesis studies first structure-guided alteration specificity towards bis-(2-hydroxyethyl) (BHET) reported here, anticipate be valuable resource further advance enzymatic plastic degradation.

Language: Английский

Citations

391
Catalytic upcycling of high-density polyethylene via a processive mechanism DOI
Akalanka Tennakoon, Xun Wu, Alexander L. Paterson

et al.

Nature Catalysis, Journal Year: 2020, Volume and Issue: 3(11), P. 893 - 901

Published: Oct. 12, 2020

Language: Английский

Citations

380
Expanding plastics recycling technologies: chemical aspects, technology status and challenges DOI Creative Commons
Houqian Li, Horacio A. Aguirre‐Villegas, Robert D. Allen

et al.

Green Chemistry, Journal Year: 2022, Volume and Issue: 24(23), P. 8899 - 9002

Published: Jan. 1, 2022

This paper reviewed the entire life cycle of plastics and options for management plastic waste to address barriers industrial chemical recycling further provide perceptions on possible opportunities with such materials.

Language: Английский

Citations

338
Enzymatic degradation of plant biomass and synthetic polymers DOI
Chun‐Chi Chen, Longhai Dai, Lixin Ma

et al.

Nature Reviews Chemistry, Journal Year: 2020, Volume and Issue: 4(3), P. 114 - 126

Published: Feb. 21, 2020

Language: Английский

Citations

315
Techno-economic, life-cycle, and socioeconomic impact analysis of enzymatic recycling of poly(ethylene terephthalate) DOI Creative Commons
Avantika Singh, Nicholas A. Rorrer, Scott Nicholson

et al.

Joule, Journal Year: 2021, Volume and Issue: 5(9), P. 2479 - 2503

Published: July 15, 2021

Esterases have emerged as important biocatalysts for enzyme-based polyester recycling of poly(ethylene terephthalate) (PET) to terephthalic acid (TPA) and ethylene glycol (EG). Here, we present process modeling, techno-economic, life-cycle, socioeconomic impact analyses an enzymatic PET depolymerization-based process, which compare with virgin TPA manufacturing. We predict that enzymatically recycled (rTPA) can be cost-competitive highlight key areas achieve this. In addition favorable long-term benefits, rTPA reduce total supply chain energy use by 69%–83% greenhouse gas emissions 17%–43% per kg TPA. An economy-wide assessment the US estimates environmental impacts up 95% while generating 45% more also relative production. Sensitivity impactful research opportunities pursue toward realizing biological upcycling.

Language: Английский

Citations

264
Enzymes’ Power for Plastics Degradation DOI
Vincent Tournier, Sophie Duquesne,

Frédérique Guillamot

et al.

Chemical Reviews, Journal Year: 2023, Volume and Issue: 123(9), P. 5612 - 5701

Published: March 14, 2023

Plastics are everywhere in our modern way of living, and their production keeps increasing every year, causing major environmental concerns. Nowadays, the end-of-life management involves accumulation landfills, incineration, recycling to a lower extent. This ecological threat environment is inspiring alternative bio-based solutions for plastic waste treatment toward circular economy. Over past decade, considerable efforts have been made degrade commodity plastics using biocatalytic approaches. Here, we provide comprehensive review on recent advances enzyme-based biocatalysis design related processes recycle or upcycle plastics, including polyesters, polyamides, polyurethanes, polyolefins. We also discuss scope limitations, challenges, opportunities this field research. An important message from that polymer-assimilating enzymes very likely part solution reaching

Language: Английский

Citations

264