The AlphaFold Protein Structure Database (AlphaFold DB, https://alphafold.ebi.ac.uk) is an openly accessible, extensive database of high-accuracy protein-structure predictions. Powered by AlphaFold v2.0 of DeepMind, it has enabled an unprecedented expansion of the structural coverage of the known protein-sequence space. AlphaFold DB provides programmatic access to and interactive visualization of predicted atomic coordinates, per-residue and pairwise model-confidence estimates and predicted aligned errors. The initial release of AlphaFold DB contains over 360,000 predicted structures across 21 model-organism proteomes, which will soon be expanded to cover most of the (over 100 million) representative sequences from the UniRef90 data set.

AlphaFold Protein Structure Database: massively expanding the structural coverage of protein-sequence space with high-accuracy models.

Plastics pollution is causing an environmental crisis, prompting the development of new approaches for recycling, and upcycling. Here, we review challenges and opportunities in chemical and biological catalysis for plastics deconstruction, recycling, and upcycling. We stress the need for rigorous characterization and use of widely available substrates, such that catalyst performance can be compared across studies. Where appropriate, we draw parallels between catalysis on biomass and plastics, as both substrates are low-value, solid, recalcitrant polymers. Innovations in catalyst design and reaction engineering are needed to overcome kinetic and thermodynamic limitations of plastics deconstruction. Either chemical and biological catalysts will need to act interfacially, where catalysts function at a solid surface, or polymers will need to be solubilized or processed to smaller intermediates to facilitate improved catalyst–substrate interaction. Overall, developing catalyst-driven technologies for plastics deconstruction and upcycling is critical to incentivize improved plastics reclamation and reduce the severe global burden of plastic waste. Plastics are invaluable materials for modern society, although they result in the generation of large amounts of litter at the end of their life cycle. This Review explores the challenges and opportunities associated with the catalytic transformation of waste plastics, looking at both chemical and biological approaches to transforming such spent materials into a resource.

Chemical and biological catalysis for plastics recycling and upcycling

The chemistry of chemical recycling of solid plastic waste via pyrolysis and gasification: State-of-the-art, challenges, and future directions

https://researchportal.port.ac.uk/portal/files/28665017/1_s2.0_S2542435121003032_main.pdf

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

Microplastics contamination is becoming a major concern worldwide. More than 1 million seabirds and 100,000 sea animals have died due to plastic contamination. In addition, plastic particles have been found in juvenile turtles. Statistical data on plastic pollution indicate that this is a serious issue. Due to their small size, microplastics have a large surface area and have more ability to absorb into biological cells. The hydrophobic surface of microplastics attracts co-contaminants such as heavy metals, pharmaceutical toxicants, flame retardants, and other plasticizers, which can then enter biological organisms. Microplastics are usually recalcitrant in the environment, causing microplastics to be transported along the food chain, with humans as the final consumer. Research has been conducted to evaluate the best way to treat and remediate microplastic pollution. Research on microplastic degradation is focused on biological and non-biological approaches. To date, microorganisms such as algae, fungi, and bacteria have attracted the attention of scientists as a tool for microplastic treatment. The degradation of microplastics is closely related to the enzymatic reactions produced by the microorganisms. Here we review microplastics degradation through enzymes from the microorganism’s perspective. We present the enzymes that have been isolated from microorganisms for specific microplastics; the mechanisms of microplastics degradation by various enzymes; and the types of microplastics for which degradation mechanisms remain unclear.

Microbial degradation of microplastics by enzymatic processes: a review

Plastics pollution represents a global environmental crisis. In response, microbes are evolving the capacity to utilize synthetic polymers as carbon and energy sources. Recently, Ideonella sakaiensis was reported to secrete a two-enzyme system to deconstruct polyethylene terephthalate (PET) to its constituent monomers. Specifically, the I. sakaiensis PETase depolymerizes PET, liberating soluble products, including mono(2-hydroxyethyl) terephthalate (MHET), which is cleaved to terephthalic acid and ethylene glycol by MHETase. Here, we report a 1.6 A resolution MHETase structure, illustrating that the MHETase core domain is similar to PETase, capped by a lid domain. Simulations of the catalytic itinerary predict that MHETase follows the canonical two-step serine hydrolase mechanism. Bioinformatics analysis suggests that MHETase evolved from ferulic acid esterases, and two homologous enzymes are shown to exhibit MHET turnover. Analysis of the two homologous enzymes and the MHETase S131G mutant demonstrates the importance of this residue for accommodation of MHET in the active site. We also demonstrate that the MHETase lid is crucial for hydrolysis of MHET and, furthermore, that MHETase does not turnover mono(2-hydroxyethyl)-furanoate or mono(2-hydroxyethyl)-isophthalate. A highly synergistic relationship between PETase and MHETase was observed for the conversion of amorphous PET film to monomers across all nonzero MHETase concentrations tested. Finally, we compare the performance of MHETase:PETase chimeric proteins of varying linker lengths, which all exhibit improved PET and MHET turnover relative to the free enzymes. Together, these results offer insights into the two-enzyme PET depolymerization system and will inform future efforts in the biological deconstruction and upcycling of mixed plastics.

https://www.pnas.org/content/pnas/117/41/25476.full.pdf

Caralyn J. Szostkiewicz

Papers

Characterization and engineering of a two-enzyme system for plastics depolymerization.

Debottlenecking 4-hydroxybenzoate hydroxylation in Pseudomonas putida KT2440 improves muconate productivity from p-coumarate.

Initiation of fatty acid biosynthesis in Pseudomonas putida KT2440.