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

Doris Ribitsch, Enrique Herrero Acero*, Katrin Julia Greimel, Anita Dellacher, Sabine Zitzenbacher, Annemarie Marold, Rosario Diaz Rodriguez, Georg Steinkellner, Karl Gruber, Helmut Schwab, Georg Gübitz

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

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
Original languageEnglish
Pages (from-to)617-629
Journale-Polymers
Volume4
Issue number1
DOIs
Publication statusPublished - 2012

Fields of Expertise

  • Human- & Biotechnology

Treatment code (Nähere Zuordnung)

  • Experimental

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