Efficient Degradation of Poly(ethylene terephthalate) with Thermobifida fusca Cutinase Exhibiting Improved Catalytic Activity Generated using Mutagenesis and Additive-based Approaches
説明
<jats:title>Abstract</jats:title><jats:p>Cutinases are promising agents for poly(ethylene terephthalate) (PET) bio-recycling because of their ability to produce the PET monomer terephthalic acid with high efficiency under mild reaction conditions. In this study, we found that the low-crystallinity PET (lcPET) hydrolysis activity of thermostable cutinase from <jats:italic>Thermobifida fusca</jats:italic> (TfCut2), was increased by the addition of cationic surfactant that attracts enzymes near the lcPET film surface via electrostatic interactions. This approach was applicable to the mutant TfCut2 G62A/F209A, which was designed based on a sequence comparison with PETase from <jats:italic>Ideonella sakaiensis</jats:italic>. As a result, the degradation rate of the mutant in the presence of cationic surfactant increased to 31 ± 0.1 nmol min<jats:sup>−1</jats:sup> cm<jats:sup>−2</jats:sup>, 12.7 times higher than that of wild-type TfCut2 in the absence of surfactant. The long-duration reaction showed that lcPET film (200 μm) was 97 ± 1.8% within 30 h, the fastest biodegradation rate of lcPET film thus far. We therefore believe that our approach would expand the possibility of enzyme utilization in industrial PET biodegradation.</jats:p>
収録刊行物
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- Scientific Reports
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Scientific Reports 9 (1), 16038-, 2019-11-05
Springer Science and Business Media LLC