Near-complete depolymerization of polyesters with nano-dispersed enzymes

Christopher DelRe, Yufeng Jiang, Philjun Kang, Junpyo Kwon, Aaron Hall, Ivan Jayapurna, Zhiyuan Ruan, Le Ma, Kyle Zolkin, Tim Li, Corinne D. Scown, Robert O. Ritchie, Thomas P. Russell and Ting Xu ()
Additional contact information
Christopher DelRe: University of California, Berkeley
Yufeng Jiang: University of California, Berkeley
Philjun Kang: University of California, Berkeley
Junpyo Kwon: Lawrence Berkeley National Laboratory
Aaron Hall: University of California, Berkeley
Ivan Jayapurna: University of California, Berkeley
Zhiyuan Ruan: University of California, Berkeley
Le Ma: University of California, Berkeley
Kyle Zolkin: University of California, Berkeley
Tim Li: University of California, Berkeley
Corinne D. Scown: Lawrence Berkeley National Laboratory
Robert O. Ritchie: University of California, Berkeley
Thomas P. Russell: Lawrence Berkeley National Laboratory
Ting Xu: University of California, Berkeley

Nature, 2021, vol. 592, issue 7855, 558-563

Abstract: Abstract Successfully interfacing enzymes and biomachinery with polymers affords on-demand modification and/or programmable degradation during the manufacture, utilization and disposal of plastics, but requires controlled biocatalysis in solid matrices with macromolecular substrates1–7. Embedding enzyme microparticles speeds up polyester degradation, but compromises host properties and unintentionally accelerates the formation of microplastics with partial polymer degradation6,8,9. Here we show that by nanoscopically dispersing enzymes with deep active sites, semi-crystalline polyesters can be degraded primarily via chain-end-mediated processive depolymerization with programmable latency and material integrity, akin to polyadenylation-induced messenger RNA decay10. It is also feasible to achieve processivity with enzymes that have surface-exposed active sites by engineering enzyme–protectant–polymer complexes. Poly(caprolactone) and poly(lactic acid) containing less than 2 weight per cent enzymes are depolymerized in days, with up to 98 per cent polymer-to-small-molecule conversion in standard soil composts and household tap water, completely eliminating current needs to separate and landfill their products in compost facilities. Furthermore, oxidases embedded in polyolefins retain their activities. However, hydrocarbon polymers do not closely associate with enzymes, as their polyester counterparts do, and the reactive radicals that are generated cannot chemically modify the macromolecular host. This study provides molecular guidance towards enzyme–polymer pairing and the selection of enzyme protectants to modulate substrate selectivity and optimize biocatalytic pathways. The results also highlight the need for in-depth research in solid-state enzymology, especially in multi-step enzymatic cascades, to tackle chemically dormant substrates without creating secondary environmental contamination and/or biosafety concerns.

Date: 2021
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DOI: 10.1038/s41586-021-03408-3

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