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image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Journal of Biotechno...arrow_drop_down
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
Journal of Biotechnology
Article . 2016 . Peer-reviewed
License: Elsevier TDM
Data sources: Crossref
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Enzymatic hydrolysis of poly(ethylene furanoate)

Authors: Pellis A.; Haernvall K.; Pichler C. M.; Ghazaryan G.; Breinbauer R.; Guebitz G. M.;

Enzymatic hydrolysis of poly(ethylene furanoate)

Abstract

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.

Country
Italy
Keywords

Enzymatic functionalization, Hydrolysis, Poly(ethylene furanoate) (PEF), Thermobifida cellulosilytica cutinase 1 (Thc_Cut1), Polyester recycling, Actinobacteria, Enzymatic hydrolysis, Bacterial Proteins, Dicarboxylic Acids, Polyethylenes, Biocatalyst, Furans, Carboxylic Ester Hydrolases, Biocatalyst; Enzymatic functionalization; Enzymatic hydrolysis; Poly(ethylene furanoate) (PEF); Polyester recycling; Thermobifida cellulosilytica cutinase 1 (Thc_Cut1); Actinobacteria; Bacterial Proteins; Carboxylic Ester Hydrolases; Dicarboxylic Acids; Hydrolysis; Furans; Polyethylenes

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Powered by OpenAIRE graph
Found an issue? Give us feedback
selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
122
Top 1%
Top 10%
Top 1%
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