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Review
. 2025 Jul 2:16:1599470.
doi: 10.3389/fmicb.2025.1599470. eCollection 2025.

Efficient biodegradation and upcycling of polyethylene terephthalate mediated by cell-factories

Fei Liu #  1 , Tao Wang #  1 , Xiao-Huan Liu  1 , Na Xu  2 , Xing-Li Pan  1
Affiliations
Review

Efficient biodegradation and upcycling of polyethylene terephthalate mediated by cell-factories

Fei Liu et al. Front Microbiol. .

Abstract

The pervasive accumulation of polyethylene terephthalate (PET) waste has emerged as a critical ecological crisis, which is mainly driven by its recalcitrance to natural degradation and widespread contamination of terrestrial and aquatic ecosystems. In response to this challenge, microbial-mediated PET biodegradation has garnered significant scientific attentions as a sustainable remediation strategy, harnessing the enzymatic cascades of specialized microorganisms to depolymerize PET into bio-assimilable monomers such as terephthalic acid (TPA) and ethylene glycol (EG). In this review, we summarize the extracellular process of PET biodegradation, including microbial attachment, colonization, and direct depolymerization, as well as the metabolic pathways of PET monomers. Strategies for developing PET-degrading chassis cells are also discussed, such as cell surface display, metabolic pathway optimization, and rational design of enzyme-PET interfaces. Microbial-enzyme consortia and molecular engineering of photosynthetic microorganisms also contribute to PET degradation. Although significant progress has been made, challenges remain in enzyme stability, metabolic bottlenecks, industrial scalability, and environmental adaptation. Overall, microbial and enzymatic strategies show great potentials in addressing PET pollution, and future interdisciplinary efforts are needed to overcome these challenges and achieve a sustainable circular plastic economy.

Keywords: PET recycling; cell factory; metabolic engineering; microbial degradation; polyethylene terephthalate; synthetic biology.

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Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

FIGURE 1
FIGURE 1
Summary of the established PET-degradation pathways.
FIGURE 2
FIGURE 2
Polyethylene terephthalate metabolic pathways and its conversion into high value chemicals.
FIGURE 3
FIGURE 3
Schematic illustration of the surface display modules for heterogeneous IsPETase expression.
FIGURE 4
FIGURE 4
Schematic illustration of the engineered curli of E. coli by fusing CsgA with IsPETase for PET degradation. (A: Construction of the whole-cell biocatalyst BINDPETase; B: strategic intracellular co-expression of PETase coupled with surface-displayed CBM3).
FIGURE 5
FIGURE 5
Schematic illustration of the high-throughput yeast surface display platform for efficient identification and evaluation of PET-degrading enzymes.
FIGURE 6
FIGURE 6
Graphic representation of surface co-display platforms with engineered PETase and MHETase on both E. coli and P. putida.
FIGURE 7
FIGURE 7
Diagrammatic representation of a robust whole-cell biocatalyst constructed with the PT-EC biocatalytic complexes displayed on the E. coli surface via coordinated Lpp-OmpA membrane fusion and SpyCatcher/SpyTag covalent immobilization.
FIGURE 8
FIGURE 8
Graphical representation of metabolic pathways involved in EG assimilation (1: oxidative reactions from EG to glyoxylate; 2: the glycerate pathway: it converts two glyoxylate molecules into two – phosphoglycerate and CO2; 3: the BHAC: a cyclic pathway where four enzymes transform two glyoxylate molecules into one oxaloacetate molecule; 4: the BHA shunt: it convertes glyoxylate and glycine into aspartate).
FIGURE 9
FIGURE 9
Graphical representation of the strategic engineering for glycerate metabolism by introducing the BHAC pathway in E. coli (A) and P. putida KT2440 (B).
FIGURE 10
FIGURE 10
Graphical representation of the co-culture of genetically modified E. coli BL21 (DE3)-LCCICCG and P. putida KT2440-ΔRDt-ΔZP46C for the biodegradation and up-cycling of PET.
FIGURE 11
FIGURE 11
Diagrammatic illustration of the engineered metabolic pathway for the bioconversion process of TPA.
FIGURE 12
FIGURE 12
Pictorial representation of PET bioconversion via the co-cultivation of engineered PETase- and PHB-producing microorganisms.
FIGURE 13
FIGURE 13
Graphic illustration of the continuous conversion of PET to muconic acid (MA) with the engineered P. putida KT2440.
FIGURE 14
FIGURE 14
Representation of the designed peptides capable of self-assembling into enzyme-like structures capable of depolymerizing PET.
FIGURE 15
FIGURE 15
The estimated synergistic degradation pathway of microbe-enzyme system.
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