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Enzymatic preparation of oligosaccharides by transglycosylation: A comparative study of glucosidases

Mangas, Juan LU and Adlercreutz, Patrick LU (2015) In Journal of Molecular Catalysis B: Enzymatic 122. p.51-55
Abstract
Five glucosidases were studied with respect to their ability to catalyse the transglycosylation of maltose or cellobiose. Experiments were carried out at high substrate concentrations to increase the ratio between transglycosylation and hydrolysis. The properties of the enzymes were quite different, and as a simple descriptor of transglycosylation ability we suggest the use of the acceptor concentration (in this case, the disaccharide concentration) required to achieve the same initial rate in transglycosylation as in hydrolysis. We call this descriptor T-50. Aspergillus niger transglucosidase had the lowest T-50 value (30 mM) and produced panose as the major product from maltose with a 69% yield after 6 h. With a longer incubation time,... (More)
Five glucosidases were studied with respect to their ability to catalyse the transglycosylation of maltose or cellobiose. Experiments were carried out at high substrate concentrations to increase the ratio between transglycosylation and hydrolysis. The properties of the enzymes were quite different, and as a simple descriptor of transglycosylation ability we suggest the use of the acceptor concentration (in this case, the disaccharide concentration) required to achieve the same initial rate in transglycosylation as in hydrolysis. We call this descriptor T-50. Aspergillus niger transglucosidase had the lowest T-50 value (30 mM) and produced panose as the major product from maltose with a 69% yield after 6 h. With a longer incubation time, secondary hydrolysis occurred and isomaltose could be obtained with a 65% yield. Aspergillus niger glucosidase was the most efficient enzyme for the transglycosylation of cellobiose with a T-50 value of 130 mM. It produced mainly cellotriose with the 1,6-linked trisaccharide (6-O-beta-glucopyranosyl-cellobiose) as a side product. Almond beta-glucosidase had a T-50 value much higher than 320 mM (the highest concentration tested), and it produced 6-O-beta-glucopyranosyl-cellobiose as the main transglycosylation product. (C) 2015 The Authors. Published by Elsevier B.V. (Less)
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organization
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Contribution to journal
publication status
published
subject
keywords
Transglucosidation, Hydrolysis, Prebiotics, Trisaccharide preparation
in
Journal of Molecular Catalysis B: Enzymatic
volume
122
pages
51 - 55
publisher
Elsevier
external identifiers
  • wos:000366078800007
  • scopus:84940928537
ISSN
1873-3158
DOI
10.1016/j.molcatb.2015.08.014
language
English
LU publication?
yes
id
c11e471d-42d4-4a9b-a78a-55bf54412db2 (old id 8557005)
date added to LUP
2016-01-26 13:31:40
date last changed
2017-10-22 03:16:46
@article{c11e471d-42d4-4a9b-a78a-55bf54412db2,
  abstract     = {Five glucosidases were studied with respect to their ability to catalyse the transglycosylation of maltose or cellobiose. Experiments were carried out at high substrate concentrations to increase the ratio between transglycosylation and hydrolysis. The properties of the enzymes were quite different, and as a simple descriptor of transglycosylation ability we suggest the use of the acceptor concentration (in this case, the disaccharide concentration) required to achieve the same initial rate in transglycosylation as in hydrolysis. We call this descriptor T-50. Aspergillus niger transglucosidase had the lowest T-50 value (30 mM) and produced panose as the major product from maltose with a 69% yield after 6 h. With a longer incubation time, secondary hydrolysis occurred and isomaltose could be obtained with a 65% yield. Aspergillus niger glucosidase was the most efficient enzyme for the transglycosylation of cellobiose with a T-50 value of 130 mM. It produced mainly cellotriose with the 1,6-linked trisaccharide (6-O-beta-glucopyranosyl-cellobiose) as a side product. Almond beta-glucosidase had a T-50 value much higher than 320 mM (the highest concentration tested), and it produced 6-O-beta-glucopyranosyl-cellobiose as the main transglycosylation product. (C) 2015 The Authors. Published by Elsevier B.V.},
  author       = {Mangas, Juan and Adlercreutz, Patrick},
  issn         = {1873-3158},
  keyword      = {Transglucosidation,Hydrolysis,Prebiotics,Trisaccharide preparation},
  language     = {eng},
  pages        = {51--55},
  publisher    = {Elsevier},
  series       = {Journal of Molecular Catalysis B: Enzymatic},
  title        = {Enzymatic preparation of oligosaccharides by transglycosylation: A comparative study of glucosidases},
  url          = {http://dx.doi.org/10.1016/j.molcatb.2015.08.014},
  volume       = {122},
  year         = {2015},
}