Enzymatic depolymerization of highly crystalline polyethylene terephthalate enabled in moist-solid reaction mixtures

• Published in: Proceedings of the National Academy of Sciences - PNAS 2021-07, Vol.118 (29), p.1-6
• Main Authors: Kaabel, Sandra, Therien, J. P. Daniel, Deschênes, Catherine E., Duncan, Dustin, Friščić, Tomislav, Auclair, Karine
• Format: Article
• Language: English
• Subjects: Amorphization; Aqueous solutions; Biocatalysis; Carboxylic Ester Hydrolases - chemistry; Catalysts; Crystal structure; Crystallinity; Cutinase; Depolymerization; Fungal Genus Humicola - enzymology; Fungal Proteins - chemistry; Hydrolysis; Physical Sciences; Plastic pollution; Plastics; Plastics - chemistry; Polyethylene; Polyethylene terephthalate; Polyethylene Terephthalates - chemistry; Polymerization; Recycling; Selectivity; Slurries; Terephthalic acid
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.2026452118

Less than 9% of the plastic produced is recycled after use, contributing to the global plastic pollution problem. While polyethylene terephthalate (PET) is one of the most common plastics, its thermomechanical recycling generates a material of lesser quality. Enzymes are highly selective, renewable catalysts active at mild temperatures; however, they lack activity toward the more crystalline forms of PET commonly found in consumer plastics, requiring the energy-expensive melt-amorphization step of PET before enzymatic depolymerization. We report here that, when used in moist-solid reaction mixtures instead of the typical dilute aqueous solutions or slurries, the cutinase from Humicola insolens can directly depolymerize amorphous and crystalline regions of PET equally, without any pretreatment, with a 13-fold higher space-time yield and a 15-fold higher enzyme efficiency than reported in prior studies with high-crystallinity material. Further, this process shows a 26-fold selectivity for terephthalic acid over other hydrolysis products.