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4.3 Degradation and modification of cellulose acetates by biological systems
Author(s) -
Puls Juergen,
Altaner Clemens,
Saake Bodo
Publication year - 2004
Publication title -
macromolecular symposia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.257
H-Index - 76
eISSN - 1521-3900
pISSN - 1022-1360
DOI - 10.1002/masy.200450409
Subject(s) - cellulose , cellulose acetate , xylan , cellulase , degradation (telecommunications) , chemistry , chitin , acetylation , hydrolysis , polysaccharide , organic chemistry , biodegradation , depolymerization , biochemistry , chitosan , telecommunications , computer science , gene
A survey is given on recent findings in the enzymology of cellulose acetate degradation. Acetyl esterases have been identified as the principal enzymes, initiating cellulose acetate degradation as a prerequisite for endoglucanase‐catalyzed cellulose acetate depolymerisation. Acetyl esterases are provided by nature to deacetylate naturally occurring partly acetylated polysaccharides, i.e. xylan and chitin. Accordingly they are not designed to attack high DS cellulose acetate. Under these circumstances acetyl esterases require a pretreatment of cellulose acetate, leading to some reduction in DS, in case highly substituted material should be degraded. One of these treatments is composting under the conditions of which a partial deacetylation may occur under the action of heat and high pH, facilitating the accessibility for acetyl esterases. However from the present knowledge it cannot be excluded that certain microbial specialists exist, being capable to degrade high DS cellulose acetate.