Reverse hydrolytic process for O-alkylation of glucose catalysed by immobilized α- and β-glucosidases

J. Kosáry, É Stefanovits-Bányai, L. Boross

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27 Citations (Scopus)


The α- and β-glucosidases showed significant O-glycosylation activity with glucose as substrate and with different alcohols both as reaction partners and solvents in reverse hydrolytic processes. With native glucosidases, upscaling resulted in low yields due to heterogeneity of reaction mixtures and the aggregation of undissolved enzymes in organic media. Immobilization of the enzymes on a modified polyacrylamide-type bead support (Acrylex C-100) increased enzyme stability resulting in higher yields and permitted to perform glucosylations on a larger scale. From these experiments O-alkyl glucosides were isolated in moderate yields. Copyright (C) 1998 Elsevier Science B.V.

Original languageEnglish
Pages (from-to)83-86
Number of pages4
JournalJournal of Biotechnology
Issue number1
Publication statusPublished - Nov 18 1998



  • Enzyme immobilization
  • O-Glycosylation
  • Reverse hydrolysis
  • α-Glucosidases
  • β-Glucosidases

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

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