Next Article in Journal
Next Article in Special Issue
Previous Article in Journal
Previous Article in Special Issue
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)

1
, 1,* , 1
, 1,2
, 1
, 1
, 3
, 1
, 1,4
, 1,2
 and 1,3
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)
View Full-Text   |   Download PDF [728 KB, uploaded 21 February 2012]   |   Browse Figures
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 enzymatic polyester functionalization; Thermobifida halotolerans esterase
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Export to BibTeX |
EndNote


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.


Polymers EISSN 2073-4360 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert