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

J. Kosáry, E. Stefanovits-Banyai, L. Boross

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

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
Volume66
Issue number1
DOIs
Publication statusPublished - Nov 18 1998

Fingerprint

Glucosidases
Alkylation
Glucose
Enzymes
Enzyme Stability
Glucosides
Glycosylation
Immobilization
Alcohols
Polyacrylates
Catalyst supports
Agglomeration
Substrates
Experiments
polyacrylamide

Keywords

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

ASJC Scopus subject areas

  • Biotechnology

Cite this

Reverse hydrolytic process for O-alkylation of glucose catalysed by immobilized α- and β-glucosidases. / Kosáry, J.; Stefanovits-Banyai, E.; Boross, L.

In: Journal of Biotechnology, Vol. 66, No. 1, 18.11.1998, p. 83-86.

Research output: Contribution to journalArticle

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