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Regioselective glycosylation of hydroquinone to alpha-arbutin by cyclodextrin glucanotransferase from Thermoanaerobacter sp.

Mathew, Sindu LU and Adlercreutz, Patrick LU (2013) In Biochemical Engineering Journal 79. p.187-193
Abstract
Hydroquinone glycosides were produced by transglycosylation reactions catalyzed by cyclodextrin glucanotransferase (CGTase) from Thermoanaerobacter sp. (Toruzyme (R) 3.0L). The reactions were carried out in an aqueous system containing hydroquinone (HQ) and maltodextrin as acceptor and donor substrate molecules respectively. The conditions for the synthesis of hydroquinone glucoside (alpha-arbutin) were 9 mM hydroquinone, maltodextrin (5%, w/v) in 20 mM citrate phosphate buffer, pH 5.5 and 0.025 mg/ml toruzyme at 40 degrees C for 24 h. The transfer efficiency of hydroquinone glycosylation was 31.8% and 29.2% respectively, when alpha-cyclodextrin and maltodextrin were employed as donor substrates. The major glycoside product was identified... (More)
Hydroquinone glycosides were produced by transglycosylation reactions catalyzed by cyclodextrin glucanotransferase (CGTase) from Thermoanaerobacter sp. (Toruzyme (R) 3.0L). The reactions were carried out in an aqueous system containing hydroquinone (HQ) and maltodextrin as acceptor and donor substrate molecules respectively. The conditions for the synthesis of hydroquinone glucoside (alpha-arbutin) were 9 mM hydroquinone, maltodextrin (5%, w/v) in 20 mM citrate phosphate buffer, pH 5.5 and 0.025 mg/ml toruzyme at 40 degrees C for 24 h. The transfer efficiency of hydroquinone glycosylation was 31.8% and 29.2% respectively, when alpha-cyclodextrin and maltodextrin were employed as donor substrates. The major glycoside product was identified as hydroquinone-1-O-alpha-D-glucopyranoside (alpha-arbutin) on the basis of mass spectrometric, nuclear magnetic resonance analysis and component analysis of its enzymatic hydrolysates. The highest molar yield of alpha-arbutin (21.2%) was obtained when alpha-cyclodextrin was used as the donor substrate. A two step enzymatic reaction system comprising of CGTase and amyloglucosidase helped to attain a molar yield of 30% for alpha-arbutin. At room temperature the solubility of alpha-arbutin in water was determined to be 12.8 g/100 ml which is approximately 1.8 fold higher than that of hydroquinone. (C) 2013 Elsevier B.V. All rights reserved. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Enzymes, Biocatalysis, Purification, Bioconversion, Arbutin, Transglycosylation
in
Biochemical Engineering Journal
volume
79
pages
187 - 193
publisher
The Association for the Study of Animal Behaviour / Elsevier B.V.
external identifiers
  • wos:000326421100024
  • scopus:84883331597
ISSN
1369-703X
DOI
10.1016/j.bej.2013.08.001
language
English
LU publication?
yes
id
57b3d3e5-01b5-40a9-858e-6379a9749f6d (old id 4209335)
date added to LUP
2014-01-07 12:53:45
date last changed
2019-03-19 02:13:49
@article{57b3d3e5-01b5-40a9-858e-6379a9749f6d,
  abstract     = {Hydroquinone glycosides were produced by transglycosylation reactions catalyzed by cyclodextrin glucanotransferase (CGTase) from Thermoanaerobacter sp. (Toruzyme (R) 3.0L). The reactions were carried out in an aqueous system containing hydroquinone (HQ) and maltodextrin as acceptor and donor substrate molecules respectively. The conditions for the synthesis of hydroquinone glucoside (alpha-arbutin) were 9 mM hydroquinone, maltodextrin (5%, w/v) in 20 mM citrate phosphate buffer, pH 5.5 and 0.025 mg/ml toruzyme at 40 degrees C for 24 h. The transfer efficiency of hydroquinone glycosylation was 31.8% and 29.2% respectively, when alpha-cyclodextrin and maltodextrin were employed as donor substrates. The major glycoside product was identified as hydroquinone-1-O-alpha-D-glucopyranoside (alpha-arbutin) on the basis of mass spectrometric, nuclear magnetic resonance analysis and component analysis of its enzymatic hydrolysates. The highest molar yield of alpha-arbutin (21.2%) was obtained when alpha-cyclodextrin was used as the donor substrate. A two step enzymatic reaction system comprising of CGTase and amyloglucosidase helped to attain a molar yield of 30% for alpha-arbutin. At room temperature the solubility of alpha-arbutin in water was determined to be 12.8 g/100 ml which is approximately 1.8 fold higher than that of hydroquinone. (C) 2013 Elsevier B.V. All rights reserved.},
  author       = {Mathew, Sindu and Adlercreutz, Patrick},
  issn         = {1369-703X},
  keyword      = {Enzymes,Biocatalysis,Purification,Bioconversion,Arbutin,Transglycosylation},
  language     = {eng},
  pages        = {187--193},
  publisher    = {The Association for the Study of Animal Behaviour / Elsevier B.V.},
  series       = {Biochemical Engineering Journal},
  title        = {Regioselective glycosylation of hydroquinone to alpha-arbutin by cyclodextrin glucanotransferase from Thermoanaerobacter sp.},
  url          = {http://dx.doi.org/10.1016/j.bej.2013.08.001},
  volume       = {79},
  year         = {2013},
}