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Eight cellulose acetate samples with degree of substitution (DS) in the range from 0.4 to 2.7 were characterised regarding their DS, substituent distribution in the anhydroglucose units, molar mass distribution and intrinsic viscosity. Samples were intensively hydrolyzed with a purified endoglucanase and the degradation monitored by analytical size exclusion chromatography (SEC). A preparative SEC...
Two cellulose acetates (CA) were regioselectively deacetylated by action of a pure Aspergillus niger acetylesterase from the carbohydrate esterase family 1. The action of acetyl esterase along the polymeric chain was monitored by a new enzyme-aided method. CA with and without esterase modification was hydrolysed with a pure endoglucanase. The fragments were deutero-acetylated and separated by preparative...
A purified acetyl esterase (AE), isolated from a commercial enzyme preparation, released acetic acid from water-soluble and water-insoluble cellulose acetates (CAs), native and chemically acetylated xylan as well as acetylated starch. The AE specifically cleaved off the acetyl substituents from the C2- and C3-positions from CAs of DS <1.8 and left the acetyl substituents at the C6-positions intact...
A screening of commercial enzyme preparations for the capability ofcellulose acetate (CA) deacetylation revealed that such enzyme activity ismore common than could be anticipated. Enzyme-aided deacetylation of celluloseacetate was clearly a function of the degree of substitution (DS). Celluloseacetates up to a DS of 1.4 were deacetylated by a large number of enzyme mixes.Interestingly, none of the...
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