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  • Transacetylations to carbohydrates catalyzed by acetylxylan esterase in the presence of organic solvent.

Transacetylations to carbohydrates catalyzed by acetylxylan esterase in the presence of organic solvent.

Biochimica et biophysica acta (2003-10-24)
Peter Biely, Ken K Y Wong, Ian D Suckling, Silvia Spániková
초록

Various conditions were applied to test the ability of acetylxylan esterase (AcXE) from Schizophyllum commune to catalyze acetyl group transfer to methyl beta-D-xylopyranoside (Me-beta-Xylp) and other carbohydrates. The best performance of the enzyme was observed in an n-hexane-vinyl acetate-sodium dioctylsulfosuccinate (DOSS)-water microemulsion at a molar water-detergent ratio (w(0)) of about 4-5. Although the enzyme was found to have a half-life of about 1 h in the system, more than 60% conversion of Me-beta-Xylp to acetylated derivatives was achieved. Under identical reaction conditions, the enzyme acetylated other carbohydrates such as methyl beta-D-cellobioside (Me-beta-Cel), cellotetraose, methyl beta-D-glucopyranoside (Me-beta-Glcp), 2-deoxy-D-glucose, D-mannose, beta-1,4-mannobiose, -mannopentaose, -mannohexaose, beta-1,4-xylobiose and -xylopentaose. This work is the first example of reverse reactions by an acetylxylan esterase and a carbohydrate esterase belonging to family 1.

MATERIALS
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Sigma-Aldrich
Methyl β-D-xylopyranoside, ≥99% (GC)