|Cote, Gregory - Greg|
Submitted to: Biotechnology International Symposium Proceedings
Publication Type: Abstract Only
Publication Acceptance Date: 8/25/1996
Publication Date: N/A
Citation: N/A Interpretive Summary:
Technical Abstract: Substrate specificities of acetylxylan esterases (AcXEs) from several microbes were investigated on partially and fully acetylated methyl glycopyranosides. AcXE from Schizophyllum commune initially removed the 3-O-acetyl group from peracetylated xylosides and glucosides, followed by slow deacetylation at other positions. Its action on peracetylated beta-mannoside yielded 4,6-di-O-Ac beta-Me-mannoside in 80% yield. By contrast, AcXE from Streptomyces lividans did not act on the mannoside, but preferentially deacetylated xylosides and glucosides at positions 2 and 3. These results provided insight pertaining to the natural function and mechanism of action of these esterases. The data also revealed the potential for these enzymes in synthetic carbohydrate chemistry, since their specificity was complementary to that of previously studied enzymes such as lipases and proteases.