Polymers 2012, 4(1), 617-629; doi:10.3390/polym4010617
Article

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

Doris Ribitsch 1 email, Enrique Herrero Acero 1,* email, Katrin Greimel 1 email, Anita Dellacher 1,2 email, Sabine Zitzenbacher 1 email, Annemarie Marold 1 email, Rosario Diaz Rodriguez 3 email, Georg Steinkellner 1 email, Karl Gruber 1,4 email, Helmut Schwab 1,2 email and Georg M. Guebitz 1,3 email
1 ACIB GmbH, Petersgasse 14, A-8010 Graz, Austria 2 Institute of Molecular Biotechnology, Graz University of Technology, A-8010 Graz, Austria 3 Institute for Environmental Biotechnology, Graz University of Technology, A-8010 Graz, Austria 4 Institute of Molecular Biosciences, University of Graz, A-8010 Graz, Austria
* Author to whom correspondence should be addressed.
Received: 31 December 2011; in revised form: 7 February 2012 / Accepted: 8 February 2012 / Published: 21 February 2012
(This article belongs to the Special Issue Enzymes in Monomer and Polymer Synthesis)
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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.
Keywords: enzymatic polyester functionalization; Thermobifida halotolerans esterase

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Cite This Article

MDPI and ACS Style

Ribitsch, D.; Herrero Acero, E.; Greimel, K.; Dellacher, A.; Zitzenbacher, S.; Marold, A.; Rodriguez, R.D.; Steinkellner, G.; Gruber, K.; Schwab, H.; Guebitz, G.M. A New Esterase from Thermobifida halotolerans Hydrolyses Polyethylene Terephthalate (PET) and Polylactic Acid (PLA). Polymers 2012, 4, 617-629.

AMA Style

Ribitsch D, Herrero Acero E, Greimel K, Dellacher A, Zitzenbacher S, Marold A, Rodriguez RD, Steinkellner G, Gruber K, Schwab H, Guebitz GM. A New Esterase from Thermobifida halotolerans Hydrolyses Polyethylene Terephthalate (PET) and Polylactic Acid (PLA). Polymers. 2012; 4(1):617-629.

Chicago/Turabian Style

Ribitsch, Doris; Herrero Acero, Enrique; Greimel, Katrin; Dellacher, Anita; Zitzenbacher, Sabine; Marold, Annemarie; Rodriguez, Rosario Diaz; Steinkellner, Georg; Gruber, Karl; Schwab, Helmut; Guebitz, Georg M. 2012. "A New Esterase from Thermobifida halotolerans Hydrolyses Polyethylene Terephthalate (PET) and Polylactic Acid (PLA)." Polymers 4, no. 1: 617-629.

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