Crowding-induced interfacial aggregation underlies enzyme concentration-dependent inhibition during poly(ethylene terephthalate) depolymerization
4 affiliations
- 1Division of Applied Life Science (BK21 Four
- 2Gyeongsang National University
- 3Anti-Aging Bio Cell Factory Regional Leading Research Center (ABC-RLRC
- 4Division of Life Science and Research Institute of Life Science
Abstract
Enzymatic depolymerization of poly(ethylene terephthalate) (PET) using PET hydrolases (PETases) offers a sustainable route for plastic recycling, yet high enzyme loadings paradoxically reduce degradation efficiency. The molecular basis of this enzyme concentration-dependent inhibition (ECDI) has remained unresolved. Here, by exploiting host-dependent differences in folding quality of a sequence-identical PETase, we show that ECDI is driven by crowding-induced interfacial aggregation, which progressively destabilizes PET-bound enzymes. By establishing aggregation propensity as a tractable design parameter, we demonstrate a complementary multi-level engineering framework operating at the sequence, folding, and reaction-environment levels that suppresses interfacial aggregation and improves PET depolymerization across multiple PETases. Our findings reveal how enzyme–enzyme interactions can govern catalytic performance at heterogeneous solid–liquid interfaces, providing a mechanistic basis for designing high-performance biocatalytic systems under high-enzyme-loading conditions.
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BibTeX
@misc{jo2026crowdinginduced,
title = {{Crowding-induced interfacial aggregation underlies enzyme concentration-dependent inhibition during poly(ethylene terephthalate) depolymerization}},
author = {Eon Ji Jo and Byung Hoon Jo},
howpublished = {ChemRxiv},
year = {2026},
month = sep,
doi = {10.26434/chemrxiv.15009159/v1},
url = {https://chemrxiv.org/doi/full/10.26434/chemrxiv.15009159/v1},
note = {CC BY-NC-ND},
}
RIS
TY - UNPB
TI - Crowding-induced interfacial aggregation underlies enzyme concentration-dependent inhibition during poly(ethylene terephthalate) depolymerization
AU - Eon Ji Jo
AU - Byung Hoon Jo
PY - 2026
DA - 2026/09/21
PB - ChemRxiv
DO - 10.26434/chemrxiv.15009159/v1
UR - https://chemrxiv.org/doi/full/10.26434/chemrxiv.15009159/v1
AB - Enzymatic depolymerization of poly(ethylene terephthalate) (PET) using PET hydrolases (PETases) offers a sustainable route for plastic recycling, yet high enzyme loadings paradoxically reduce degradation efficiency. The molecular basis of this enzyme concentration-dependent inhibition (ECDI) has remained unresolved. Here, by exploiting host-dependent differences in folding quality of a sequence-identical PETase, we show that ECDI is driven by crowding-induced interfacial aggregation, which progressively destabilizes PET-bound enzymes. By establishing aggregation propensity as a tractable design parameter, we demonstrate a complementary multi-level engineering framework operating at the sequence, folding, and reaction-environment levels that suppresses interfacial aggregation and improves PET depolymerization across multiple PETases. Our findings reveal how enzyme–enzyme interactions can govern catalytic performance at heterogeneous solid–liquid interfaces, providing a mechanistic basis for designing high-performance biocatalytic systems under high-enzyme-loading conditions.
ER -