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  • M. Hajighasemi
    University of Toronto, Canada
  • Boguslaw P. Nocek
    Argonne National Laboratory, Argonne, Illinois
  • Anatoli Tchigvintsev
    University of Toronto, Canada
  • Greg Brown,
    University of Toronto, Canada
  • Robert Flick
    University of Toronto, Canada
  • Xiaohui Xu
    University of Toronto, Canada
  • Hong Cui
    University of Toronto, Canada
  • Tran Hai
  • Andrzej Joachimiak
    Argonne National Laboratory, Argonne, Illinois
  • Peter Golyshin
  • Alexei Savchenko
    University of Toronto, Canada
  • Elizabeth A. Edwards
    University of Toronto, Canada
  • A. F. Yakunin
    University of Toronto, Canada
Polylactic acid (PLA) is a biodegradable polyester derived from renewable resources, which is a leading candidate for the replacement of traditional petroleum-based polymers. Since the global production of PLA is quickly growing, there is an urgent need for the development of efficient recycling technologies, which will produce lactic acid instead of CO2 as the final product. After screening 90 purified microbial α/β-hydrolases, we identified hydrolytic activity against emulsified PLA in two uncharacterized proteins, ABO2449 from Alcanivorax borkumensis and RPA1511 from Rhodopseudomonas palustris. Both enzymes were also active against emulsified polycaprolactone and other polyesters, as well as against soluble α-naphthyl and p-nitrophenyl monoesters. In addition, both ABO2449 and RPA1511 catalyzed complete or extensive hydrolysis of solid PLA with the production of lactic acid monomers, dimers, and larger oligomers as products. The crystal structure of RPA1511 was determined at 2.2 Å resolution and revealed a classical α/β-hydrolase fold with a wide-open active site containing a molecule of polyethylene glycol bound near the catalytic triad Ser114-His270-Asp242. Site-directed mutagenesis of both proteins demonstrated that the catalytic triad residues are important for the hydrolysis of both monoester and polyester substrates. We also identified several residues in RPA1511 (Gln172, Leu212, Met215, Trp218, and Leu220) and ABO2449 (Phe38 and Leu152), which were not essential for activity against soluble monoesters, but were found to be critical for the hydrolysis of PLA. Our results indicate that microbial carboxyl esterases can efficiently hydrolyze various polyesters making them attractive biocatalysts for plastics depolymerization and recycling.
Original languageEnglish
Pages (from-to)2027-2039
Issue number6
Publication statusPublished - 18 Apr 2016

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