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Engineering the PETase Enzyme for More Efficient Degradation of PET Plastic
Author(s) -
Rupert Allison,
Khong Trang,
Duplan Amanda,
Fenton Robin,
Hall Bonnie
Publication year - 2021
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2021.35.s1.04655
Subject(s) - polyethylene terephthalate , polyester , degradation (telecommunications) , plastic pollution , polymer , materials science , polyethylene glycol , polyethylene , plastic waste , chemistry , chemical engineering , composite material , organic chemistry , waste management , computer science , environmental chemistry , engineering , telecommunications , microplastics
Polyethylene terephthalate (PET) is the most common type of plastic in the world and plays a major role in plastic pollution. PET's polyester resin structure makes it highly resistant to degradation, allowing it to remain in landfills and contribute to overall plastic accumulation. Yoshida et al. identified the PETase enzyme as being able to break down PET plastic into four major products: BHET and MHET (small polymer fragments), and the original starting materials ethylene glycol and TPA. Large‐scale plastic degradation is not currently feasible, however, due to the enzyme's low efficiency. The goal of our research is to engineer the PETase enzyme to work more efficiently at breaking down PET plastic. PETase was overexpressed, FPLC‐purified, and its activity analyzed using HPLC. Computational design of engineered mutants was performed, and these mutants were analyzed in parallel with wild‐type PETase. Our hope is that engineering a higher efficiency PETase for use in plastic degradation and recycling can help reduce the world's plastic waste.