Literature DB >> 14572903

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

Peter Biely1, Ken K Y Wong, Ian D Suckling, Silvia Spániková.   

Abstract

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.

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Year:  2003        PMID: 14572903     DOI: 10.1016/s0304-4165(03)00154-5

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  1 in total

1.  Cloning, overexpression in Escherichia coli, and characterization of a thermostable fungal acetylxylan esterase from Talaromyces emersonii.

Authors:  Deborah M Waters; Patrick G Murray; Yuta Miki; Angel T Martínez; Maria G Tuohy; Craig B Faulds
Journal:  Appl Environ Microbiol       Date:  2012-03-09       Impact factor: 4.792

  1 in total

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