, Volume 10, Issue 1, pp 85–95

Specificity of an Aspergillus Niger Esterase Deacetylating Cellulose Acetate


DOI: 10.1023/A:1023010330865

Cite this article as:
Altaner, C., Saake, B. & Puls, J. Cellulose (2003) 10: 85. doi:10.1023/A:1023010330865


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 without degrading the polysaccharide. The activity of endoglucanase was enhanced by the presence of acetyl esterase, while the acetyl esterase derived no advantage from the presence of the endoglucanase; it was able to function independently.

Acetylated xylanAcetyl esteraseAspergillus nigerCellulose acetateEndoglucanaseRegioselective deacetylationSubstrate inhibition

Copyright information

© Kluwer Academic Publishers 2003

Authors and Affiliations

  1. 1.Institute for Wood Chemistry and Chemical Technology of WoodFederal Research Centre for Forestry and Forest ProductsHamburgGermany