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<p>Enzymatic depolymerization of polyethylene terephthalate (PET), the world’s most widely used polyester, in seawater at ambient temperature offers a promising and energy-efficient route for freshwater-free plastic recycling. While a number of PET hydrolases have been reported in recent years, their potential under saline conditions remains largely unexplored. Here, we screened eight enzymes in artificial seawater at 30&#xa0;°C and engineered the most active one, <i>Is</i>PETase, using a semi-rational strategy focused on rigidifying flexible sites. The resulting variant M8 showed simultaneous enhancementsin thermostability (ΔT<sub>m</sub> = + 27.3&#xa0;°C), activity (1.14-fold increase) and soluble expression yield (14.3-fold increase). The overall depolymerization efficiency of M8 surpassed that of the thermostable benchmark enzymes DuraPETase and LCC-ICCG by 32.2- and 10.4-fold, respectively. Notably, M8 achieved continuous and efficient depolymerization of 15% (w/v) PET powder in natural seawater at 37&#xa0;°C, yielding monomers at a rate of 15.4&#xa0;mM/day, a concentration sufficient to support downstream bacterial assimilation. This work provides an efficient enzymatic platform and paves the way for fully integrated, seawater-based plastic bioconversion processes.</p>

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Engineering a robust IsPETase for energy-efficient PET depolymerization in natural seawater at ambient temperatures

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年4月15日

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  • Xin Huang,
  • Qian Jia,
  • Guang Li,
  • Xiangpeng Yang,
  • Shujing Xu,
  • Jianzhong Liu,
  • Wenjun Li,
  • Yuhuan Liu,
  • Wei Xie,
  • Lichuang Cao

摘要

Enzymatic depolymerization of polyethylene terephthalate (PET), the world’s most widely used polyester, in seawater at ambient temperature offers a promising and energy-efficient route for freshwater-free plastic recycling. While a number of PET hydrolases have been reported in recent years, their potential under saline conditions remains largely unexplored. Here, we screened eight enzymes in artificial seawater at 30 °C and engineered the most active one, IsPETase, using a semi-rational strategy focused on rigidifying flexible sites. The resulting variant M8 showed simultaneous enhancementsin thermostability (ΔTm = + 27.3 °C), activity (1.14-fold increase) and soluble expression yield (14.3-fold increase). The overall depolymerization efficiency of M8 surpassed that of the thermostable benchmark enzymes DuraPETase and LCC-ICCG by 32.2- and 10.4-fold, respectively. Notably, M8 achieved continuous and efficient depolymerization of 15% (w/v) PET powder in natural seawater at 37 °C, yielding monomers at a rate of 15.4 mM/day, a concentration sufficient to support downstream bacterial assimilation. This work provides an efficient enzymatic platform and paves the way for fully integrated, seawater-based plastic bioconversion processes.