The role of binding modules in enzymatic poly(ethylene terephthalate) hydrolysis at high-solids loadings

In nature, enzymes that deconstruct biological polymers, such as cellulose and chitin, often exhibit multi-domain architectures, comprising a catalytic domain non-catalytic binding module; the latter serves to increase enzyme concentration at substrate surface. This architecture has been shown improve hydrolysis of poly(ethylene terephthalate) (PET) using engineered cutinase enzymes. Here, we examine role accessory modules industrially relevant PET solids loadings necessary for cost-effective enzymatic recycling. Using thermostable variant leaf compost (LCC), produced synthetic fusion constructs LCC with five type A carbohydrate-binding (CBMs). At below 10 wt %, CBMs aromatic monomer yield from PET, but above this threshold, conversion extents up 97% are reached no added benefits presence CBM fusions. suggests herein studied not industrial • new exhibits higher thermostability greater turnover Specific stimulate low-solids loading The advantage these is lost high-solids Closed-loop recycling open-loop upcycling waste plastics represent suite critical technologies address plastic-waste pollution crisis. Enzymatic deconstruction polyester among several options available chemical common plastic. While early demonstrations have feasibility, technology yet cost competitive production virgin petroleum-derived PET. study analyzes an engineering approach takes lesson nature efficiency PET-hydrolyzing evaluates impact strategy under reaction conditions simulate key feature implications can help focus resources field on solutions enable rapid deployment viable realistically pollution. offers promising solution global plastic problem. Research into domains enhance so far tested high loadings. show do offer any benefit industrial-scale biorecycling.