Journal
JOURNAL OF BIOTECHNOLOGY
Volume 235, Issue -, Pages 47-53Publisher
ELSEVIER
DOI: 10.1016/j.jbiotec.2016.02.006
Keywords
Thermobifida cellulosilytica cutinase 1 (Thc_Cut1); Enzymatic functionalization; Poly(ethylene furanoate) (PEF); Enzymatic hydrolysis; Polyester recycling; Biocatalyst
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Funding
- European Union [289253]
- Federal Ministry of Science, Research and Economy (BMWFW)
- Federal Ministry of Traffic, Innovation and Technology (bmvit)
- Styrian Business Promotion Agency SFG
- Standortagentur Tirol
- Government of Lower Austria
- ZIT-Technology Agency of the City of Vienna through the COMET-Funding Program
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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 40 kDa) 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. (C) 2016 Elsevier B.V. All rights reserved.
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