Enzymatic hydrolysis of poly(ethylene furanoate).

Pellis A; Haernvall K; Pichler CM; Ghazaryan G; Breinbauer R; Guebitz GM

doi:10.1016/j.jbiotec.2016.02.006

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Journal article

Enzymatic hydrolysis of poly(ethylene furanoate).

Pellis A BOKU-University of Natural Resources and Life Sciences, Institute for Environmental Biotechnology, Konrad Lorenz Strasse 20, 3430, Tulln an der Donau, Austria. Electronic address: alessandro.pellis@boku.ac.at.
Haernvall K ACIB-Austrian Centre of Industrial Biotechnology GmbH, Konrad Lorenz Strasse 20, 3430, Tulln an der Donau, Austria.
Pichler CM Graz University of Technology, Institute of Organic Chemistry, Stremayrgasse 9, 8010 Graz, Austria.
Ghazaryan G Department of Materials, Swiss Federal Institute of Technology Zurich (ETH Zurich), Polymer Technology, Vladimir-Prelog-Weg 5, 8093 Zurich, Switzerland; Laboratory for Biointerfaces, Swiss Federal Laboratories for Materials Science and Technology (Empa), Lerchenfeldstrasse 5, 9014 St. Gallen, Switzerland.
Breinbauer R Graz University of Technology, Institute of Organic Chemistry, Stremayrgasse 9, 8010 Graz, Austria.
Guebitz GM BOKU-University of Natural Resources and Life Sciences, Institute for Environmental Biotechnology, Konrad Lorenz Strasse 20, 3430, Tulln an der Donau, Austria; ACIB-Austrian Centre of Industrial Biotechnology GmbH, Konrad Lorenz Strasse 20, 3430, Tulln an der Donau, Austria.

2016-02-09

Published in:

Journal of biotechnology. - 2016

Poly(ethylene furanoate) (PEF)

Thermobifida cellulosilytica cutinase 1 (Thc_Cut1)

English The urgency of producing new environmentally-friendly polyesters strongly enhanced the development of bio-based poly(ethylene furanoate) (PEF) as an alternative to plastics like poly(ethylene terephthalate) (PET) for applications that include food packaging, personal and home care containers and thermoforming equipment. In this study, PEF powders of various molecular weights (6, 10 and 40kDa) were synthetized and their susceptibility to enzymatic hydrolysis was investigated for the first time. According to LC/TOF-MS analysis, cutinase 1 from Thermobifida cellulosilytica liberated both 2,5-furandicarboxylic acid and oligomers of up to DP4. The enzyme preferentially hydrolyzed PEF with higher molecular weights but was active on all tested substrates. Mild enzymatic hydrolysis of PEF has a potential both for surface functionalization and monomers recycling.

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