A New Esterase from Thermobifida halotolerans Hydrolyses Polyethylene Terephthalate (PET) and Polylactic Acid (PLA)

Polymers - Tập 4 Số 1 - Trang 617-629
Doris Ribitsch1, Enrique Herrero Acero1, Katrin Julia Greimel1, Anita Dellacher1,2, Sabine Zitzenbacher1, Annemarie Marold1, Rosario Díaz Rodríguez3, Georg Steinkellner1, Karl Gruber1,4, Helmut Schwab1,2, Georg M. Guebitz1,3
1ACIB GmbH, Petersgasse 14, A-8010 Graz, Austria
2Institute of Molecular Biotechnology, Graz University of Technology, A-8010 Graz, Austria
3Institute for Environmental Biotechnology, Graz University of Technology, A-8010 Graz, Austria
4Institute of Molecular Biosciences, University of Graz, A-8010 Graz, Austria

Tóm tắt

A new esterase from Thermobifida halotolerans (Thh_Est) was cloned and expressed in E. coli and investigated for surface hydrolysis of polylactic acid (PLA) and polyethylene terephthalate (PET). Thh_Est is a member of the serine hydrolases superfamily containing the -GxSxG- motif with 85–87% homology to an esterase from T. alba, to an acetylxylan esterase from T. fusca and to various Thermobifida cutinases. Thh_Est hydrolyzed the PET model substrate bis(benzoyloxyethyl)terephthalate and PET releasing terephthalic acid and mono-(2-hydroxyethyl) terephthalate in comparable amounts (19.8 and 21.5 mmol/mol of enzyme) while no higher oligomers like bis-(2-hydroxyethyl) terephthalate were detected. Similarly, PLA was hydrolyzed as indicated by the release of lactic acid. Enzymatic surface hydrolysis of PET and PLA led to a strong hydrophilicity increase, as quantified with a WCA decrease from 90.8° and 75.5° to 50.4° and to a complete spread of the water drop on the surface, respectively.

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