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Open AccessArticle

Enzymatic Systems for Cellulose Acetate Degradation

Institute of Environmental Biotechnology, University of Natural Resources and Life Sciences Vienna, Konrad-Lorenz-Strasse 20, 3430 Tulln an der Donau, Austria
Chemical Wood Technology, Department of Wood Science, University of Hamburg, Leuschnerstrasse 91, 21031 Hamburg, Germany
Department of Food Science and Technology, University of Natural Resources and Life Sciences Vienna, Muthgasse 18, 1190 Vienna, Austria
R. J. Reynolds Tobacco Company, 401 North Main Street, Winston-Salem, NC 27101, USA
Author to whom correspondence should be addressed.
Catalysts 2017, 7(10), 287;
Received: 13 August 2017 / Revised: 25 September 2017 / Accepted: 25 September 2017 / Published: 27 September 2017
(This article belongs to the Special Issue Biocatalysis and Biotransformations)
PDF [2411 KB, uploaded 27 September 2017]


Cellulose acetate (CA)-based materials, like cigarette filters, contribute to landscape pollution challenging municipal authorities and manufacturers. This study investigates the potential of enzymes to degrade CA and to be potentially incorporated into the respective materials, enhancing biodegradation. Deacetylation studies based on Liquid Chromatography-Mass Spectrometry-Time of Flight (LC-MS-TOF), High Performance Liquid Chromatography (HPLC), and spectrophotometric analysis showed that the tested esterases were able to deacetylate the plasticizer triacetin (glycerol triacetate) and glucose pentaacetate (cellulose acetate model compound). The most effective esterases for deacetylation belong to the enzyme family 2 (AXE55, AXE 53, GAE), they deacetylated CA with a degree of acetylation of up to 1.8. A combination of esterases and cellulases showed synergistic effects, the absolute glucose recovery for CA 1.8 was increased from 15% to 28% when an enzymatic deacetylation was performed. Lytic polysaccharide monooxygenase (LPMO), and cellobiohydrolase were able to cleave cellulose acetates with a degree of acetylation of up to 1.4, whereas chitinase showed no activity. In general, the degree of substitution, chain length, and acetyl group distribution were found to affect CA degradation. This study shows that, for a successful enzyme-based deacetylation system, a cocktail of enzymes, which will randomly cleave and generate shorter CA fragments, is the most suitable. View Full-Text
Keywords: cellulose acetate; esterase; cellulase; polysaccharide monooxygenase; chitinase; cellobiohydrolase; deacetylation; hydrolysis cellulose acetate; esterase; cellulase; polysaccharide monooxygenase; chitinase; cellobiohydrolase; deacetylation; hydrolysis

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Haske-Cornelius, O.; Pellis, A.; Tegl, G.; Wurz, S.; Saake, B.; Ludwig, R.; Sebastian, A.; Nyanhongo, G.S.; Guebitz, G.M. Enzymatic Systems for Cellulose Acetate Degradation. Catalysts 2017, 7, 287.

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