Class I hydrophobins pretreatment stimulates PETase for monomers recycling of waste PETs
نویسندگان
چکیده
Poly(ethylene terephthalate) hydrolase (PETase) from Ideonella sakaiensis 201-F6 was expressed and purified Escherichia coli to hydrolyze poly(ethylene (PET) fibers waste for its monomers recycling. Hydrolysis carried out at pH 8 30 °C found be the optimal condition based on measured monomer mono(2-hydroxyethyl) terephthalate (MHET) terephthalic acid (TPA) concentrations after 24 h reaction. The intermediate product bis(2-hydroxyethyl) (BHET) a good substrate PETase because BHET released PET hydrolysis efficiently converted into MHET. Only trace amount of MHET could further hydrolyzed TPA. Class I hydrophobins RolA Aspergillus oryzae HGFI Grifola frondosa were E. pretreat surface accelerating against PET. weight loss increased approximately 18% 34% pretreatment. releases TPA HGFI-pretreated enhanced 48% 62%, respectively. selectivity (TPA/MHET ratio) reaction 0.5. • successfully in . optimum conditions by wild °C. Hydrophobins pretreatment releasing monomers.
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ژورنال
عنوان ژورنال: International Journal of Biological Macromolecules
سال: 2021
ISSN: ['1879-0003', '0141-8130']
DOI: https://doi.org/10.1016/j.ijbiomac.2021.02.026