# Ethylene Glycol‐Guided Enhancement of Bis(2‐Hydroxyethyl) Terephthalic Acid as a Primary Product of Enzymatic Poly(Ethylene Terephthalate) Depolymerization

**Authors:** Tobias S. Radmer, Thore B. Thomsen, Leon T. Krinn, Anne S. Meyer

PMC · DOI: 10.1002/cssc.202502346 · Chemsuschem · 2026-03-19

## TL;DR

This study shows how adding ethylene glycol can boost the production of a key recycling product during enzymatic breakdown of PET plastic.

## Contribution

The novel finding is that ethylene glycol enhances BHET yield by altering enzyme behavior on PET surfaces.

## Key findings

- Adding 27–29% ethylene glycol maximizes BHET production using the LCCICCG enzyme.
- Ethylene glycol reduces the lag phase of enzymatic reactions and lessens the impact of PET crystallinity.
- EG affects enzyme adsorption, increasing substrate affinity and directing enzyme activity to the liquid phase.

## Abstract

Recycling of enzymatically depolymerized poly(ethylene terephthalate) (PET) involves polycondensation of bis(2‐hydroxy‐ethyl) terephthalic acid (BHET)—a degradation product of enzymatic PET hydrolysis. The recycling process is simplified when more BHET is generated by the enzymatic reaction. Here, we report how ethylene glycol (EG) addition can maximize BHET formation using leading PET hydrolases, LCCICCG, and PHL7. EG at any level above 2–5% vol/vol was found to decrease the steady‐state enzymatic degradation rates while enhancing the relative production of BHET. For LCCICCG, the highest measured BHET levels (product fraction approaching 0.5) were attained at EG levels of ∼27–29% and reaction temperature ∼62.5°C. EG shortened the enzymatic reaction lag‐phase and lowered the lag‐phase increase with PET crystallinity. EG works by perturbing the adsorption, including nonproductive adsorption, of the enzymes to the PET surface, which manifests as an apparent change in substrate affinity (increases the inv
K
m in interfacial kinetics modeling) and directs the enzyme more to the liquid phase.

Optimizing BHET product levels by ethylene glycol content during enzymatic degradation of Poly(Ethylene Terephthalate) with the enzyme LCCICCG. © 2026 WILEY‐VCH GmbH

## Linked entities

- **Chemicals:** ethylene glycol (PubChem CID 174), bis(2-hydroxyethyl) terephthalic acid (PubChem CID 21863479)

## Full-text entities

- **Genes:** SNORD118 (small nucleolar RNA, C/D box 118) [NCBI Gene 727676] {aka LCC, U8}, PODXL2 (podocalyxin like 2) [NCBI Gene 50512] {aka EG, PODLX2}
- **Chemicals:** water (MESH:D014867), Glycine (MESH:D005998), formic acid (MESH:C030544), acetonitrile (MESH:C032159), PET (MESH:D011093), EG (MESH:D019855), TPA (MESH:C011363), methanol (MESH:D000432), bis(benzoyloxyethyl)terephthalate (MESH:C546855), NaOH (MESH:D012972), BHET (MESH:C110732), polymer (MESH:D011108), BHET (-), T (MESH:D014316)
- **Species:** Pseudideonella sakaiensis (species) [taxon 1547922]

## Full text

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## Figures

11 figures with captions in the complete paper: https://tomesphere.com/paper/PMC13000671/full.md

## References

20 references — full list in the complete paper: https://tomesphere.com/paper/PMC13000671/full.md

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Source: https://tomesphere.com/paper/PMC13000671