Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 61, Issue 37, Pages -Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202203061
Keywords
Bioinformatics; Degradation; Genetic Code Expansion; Hydrolases; Plastics
Categories
Funding
- VISTEC
- Wellcome Trust [217249/Z/19/Z]
- National Research Council of Thailand [MRG6280177]
- Thailand Science Research and Innovation (Global Partnership Program from Program Management Unit-B)
- PTT Innovation Institute
- ALSAC
- Wellcome Trust [217249/Z/19/Z] Funding Source: Wellcome Trust
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We report the discovery of a new PET hydrolase, named MG8, from the human saliva metagenome. MG8 exhibits robust PET degradation activities under different conditions and outperforms other hydrolases in degrading PET. Furthermore, we genetically modified MG8 to serve as a covalent binder for PET functionalization, enabling the attachment of protein cargos to PET and other polyester plastics.
We report a bioinformatic workflow and subsequent discovery of a new polyethylene terephthalate (PET) hydrolase, which we named MG8, from the human saliva metagenome. MG8 has robust PET plastic degradation activities under different temperature and salinity conditions, outperforming several naturally occurring and engineered hydrolases in degrading PET. Moreover, we genetically encoded 2,3-diaminopropionic acid (DAP) in place of the catalytic serine residue of MG8, thereby converting a PET hydrolase into a covalent binder for bio-functionalization of PET. We show that MG8(DAP), in conjunction with a split green fluorescent protein system, can be used to attach protein cargos to PET as well as other polyester plastics. The discovery of a highly active PET hydrolase from the human metagenome-currently an underexplored resource for industrial enzyme discovery-as well as the repurposing of such an enzyme into a plastic functionalization tool, should facilitate ongoing efforts to degrade and maximize reusability of PET.
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