Design and construction of chemical-biological module clusters for degradation and assimilation of poly(ethylene terephthalate) waste

J Environ Manage. 2024 Jun:361:121258. doi: 10.1016/j.jenvman.2024.121258. Epub 2024 May 29.

Abstract

The rising accumulation of poly(ethylene terephthalate) (PET) waste presents an urgent ecological challenge, necessitating an efficient and economical treatment technology. Here, we developed chemical-biological module clusters that perform chemical pretreatment, enzymatic degradation, and microbial assimilation for the large-scale treatment of PET waste. This module cluster included (i) a chemical pretreatment that involves incorporating polycaprolactone (PCL) at a weight ratio of 2% (PET:PCL = 98:2) into PET via mechanical blending, which effectively reduces the crystallinity and enhances degradation; (ii) enzymatic degradation using Thermobifida fusca cutinase variant (4Mz), that achieves complete degradation of pretreated PET at 300 g/L PET, with an enzymatic loading of 1 mg protein per gram of PET; and (iii) microbial assimilation, where Rhodococcus jostii RHA1 metabolizes the degradation products, assimilating each monomer at a rate above 90%. A comparative life cycle assessment demonstrated that the carbon emissions from our module clusters (0.25 kg CO2-eq/kg PET) are lower than those from other established approaches. This study pioneers a closed-loop system that seamlessly incorporates pretreatment, degradation, and assimilation processes, thus mitigating the environmental impacts of PET waste and propelling the development of a circular PET economy.

Keywords: Chemical pretreatment; Enzymatic degradation; Mechanical blending method; Microbial assimilation; Polycaprolactone.

MeSH terms

  • Biodegradation, Environmental*
  • Carboxylic Ester Hydrolases
  • Polyesters* / chemistry
  • Polyesters* / metabolism
  • Polyethylene Terephthalates* / chemistry
  • Polyethylene Terephthalates* / metabolism

Substances

  • Polyethylene Terephthalates
  • Polyesters
  • polycaprolactone
  • cutinase
  • Carboxylic Ester Hydrolases