|Biely, Peter - INST OF CHEMISTRY|
|Kluepfel, D - UNIV DU QUEBEC|
Submitted to: Pacific Basin Society Chemical International Congress Abstracts
Publication Type: Abstract Only
Publication Acceptance Date: December 17, 1995
Publication Date: N/A
Technical Abstract: Acetylxylan esterases are enzymes which, in contrast to other esterases and lipases, show high affinity towards partially acetylated hardwood 4-O-methyl-glucuronoxylan. The substrate specificity of these enzymes has not been investigated and it is unknown how these enzymes perform on other acetylated carbohydrates. Two xylanase-free enzyme preparations were examined on a variety of acetylated polysaccharides and mono- and oligosaccharides. The acetylxylan esterase of Streptomyces lividans (Shareck et al., Gene 153, ..., 1995) which seems to have a substrate-binding domain, practically did not attack other available substrates, therefore, the enzyme appears to be very specific for the polysaccharide. On the other hand, acetylxylan esterase from Schizophyllum commune was capable of rapid partial deacetylation of per-O-acetyl-D-glucose, -D-xylose and -sucrose. However, the enzyme showed poor activity on acetylated polysaccharides that were insoluble in water. The results indicate that the acetylxylan esterase will perform on variety of acetylated substrates which are at least partially water-soluble.