{
  "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.",
  "abstract_shown": true,
  "affiliations": [
    "Division of Applied Life Science (BK21 Four",
    "Gyeongsang National University",
    "Anti-Aging Bio Cell Factory Regional Leading Research Center (ABC-RLRC",
    "Division of Life Science and Research Institute of Life Science"
  ],
  "article_type": null,
  "arxiv": null,
  "author_total": 2,
  "authors": [
    {
      "affs": [
        0,
        1,
        2
      ],
      "name": "Eon Ji Jo"
    },
    {
      "affs": [
        0,
        1,
        2,
        3
      ],
      "name": "Byung Hoon Jo"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/a6xz5qfh71xvj.bib",
  "cited_by": 0,
  "doi": "10.26434/chemrxiv.15009159/v1",
  "fulltext_url": null,
  "id": "a6xz5qfh71xvj",
  "issns": [],
  "landing_url": "https://chemrxiv.org/doi/full/10.26434/chemrxiv.15009159/v1",
  "language": null,
  "licence": "CC-BY-NC-ND",
  "licence_label": "CC BY-NC-ND",
  "licence_source": "journal",
  "licence_url": "https://creativecommons.org/licenses/by-nc-nd/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "openalex",
      "1312|Enzyme Catalysis and Immobilization"
    ]
  ],
  "openalex": "W7213955373",
  "pdf_url": "https://chemrxiv.org/doi/pdf/10.26434/chemrxiv.15009159/v1",
  "pmcid": null,
  "pmid": null,
  "published": "2026-09-21",
  "publisher": "American Chemical Society (ACS)",
  "ris": "https://research.draconitic.com/paper/a6xz5qfh71xvj.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:19Z",
      "native_id": "10.26434/chemrxiv.15009159",
      "source": "chemrxiv",
      "url": "https://chemrxiv.org/doi/full/10.26434/chemrxiv.15009159/v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "openalex:1312|Enzyme Catalysis and Immobilization",
      "subfield": "molecular-biology"
    }
  ],
  "title": "Crowding-induced interfacial aggregation underlies enzyme concentration-dependent inhibition during poly(ethylene terephthalate) depolymerization",
  "title_text": "Crowding-induced interfacial aggregation underlies enzyme concentration-dependent inhibition during poly(ethylene terephthalate) depolymerization",
  "type": "preprint",
  "updated_at": "2026-10-30T12:17:19Z",
  "url": "https://research.draconitic.com/paper/a6xz5qfh71xvj",
  "venue": "ChemRxiv",
  "versions": []
}