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Gewählte Publikation:

Haske-Cornelius, O; Pellis, A; Tegl, G; Wurz, S; Saake, B; Ludwig, R; Sebastian, A; Nyanhongo, GS; Guebitz, GM.
(2017): Enzymatic Systems for Cellulose Acetate Degradation
CATALYSTS. 2017; 7(10): FullText FullText_BOKU

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.
Autor/innen der BOKU Wien:
Gübitz Georg
Haske-Cornelius Oskar
Ludwig Roland
Nyanhongo Gibson Stephen
Pellis Alessandro
Tegl Gregor Franz
Wurz Stefan
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Find related publications in this database (Keywords)
cellulose acetate
polysaccharide monooxygenase

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