Engineering a robust IsPETase for energy-efficient PET depolymerization in natural seawater at ambient temperatures
= + 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.
Authors
- Xiangpeng Yang (ORCID: https://orcid.org/0000-0001-7009-1532)
- Xin Huang (ORCID: https://orcid.org/0000-0002-7253-543X)
- Shuqi Xu (ORCID: https://orcid.org/0000-0002-9615-7533)
- Wenhua Li (ORCID: https://orcid.org/0000-0002-9457-6662)
- Wei Xie
- Jianzhong Liu
- Qian Jia
Institutions
- Sun Yat-sen University (CN)
Publication Details
- Journal
- Advanced Biotechnology
- Published
- 2026-04-15
- DOI
- https://doi.org/10.1007/s44307-026-00104-z
- Primary Topic
- Microplastics and Plastic Pollution
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- Salt Science Research Foundation
- National Supercomputer Centre in Guangzhou
- National Natural Science Foundation of China
- Chinese Academy of Sciences
- Guangzhou Municipal Science and Technology Bureau
- South China Sea Institute of Oceanology, Chinese Academy of Sciences
- Institute of Oceanology, Chinese Academy of Sciences
- National Key Research and Development Program of China