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Enzymatic synthesis of piceid glycosides by cyclodextrin glucanotransferase

Mathew, Sindhu; Hedström, Martin LU and Adlercreutz, Patrick LU (2012) In Process Biochemistry 47(3). p.528-532
Abstract
Novel glycosides of piceid (3,4'-5-trihydroxy stilbene 3-O-beta-D-glucoside) were produced by the transglycosylation reactions of cyclodextrin glucanotransferase (CGTase) from Bacillus macerans, with piceid (PicG(1)) and maltodextrin as the acceptor and donor substrates, respectively. The reactions were performed at 40 degrees C with 2.56 mM piceid (0.1% w/v) and maltodextrin (5% w/v) in 0.02 M citrate phosphate buffer, pH 6.0 containing 5% (v/v) methanol for 6h. Glucose, maltose, sucrose, maltotriose and alpha-cyclodextrin (alpha-CD) were also used to analyze their ability to function as donor substrates, for the glycosylation of piceid. Among the different donor substrates used, the maximum transfer efficiency (TE) of glycosylation of... (More)
Novel glycosides of piceid (3,4'-5-trihydroxy stilbene 3-O-beta-D-glucoside) were produced by the transglycosylation reactions of cyclodextrin glucanotransferase (CGTase) from Bacillus macerans, with piceid (PicG(1)) and maltodextrin as the acceptor and donor substrates, respectively. The reactions were performed at 40 degrees C with 2.56 mM piceid (0.1% w/v) and maltodextrin (5% w/v) in 0.02 M citrate phosphate buffer, pH 6.0 containing 5% (v/v) methanol for 6h. Glucose, maltose, sucrose, maltotriose and alpha-cyclodextrin (alpha-CD) were also used to analyze their ability to function as donor substrates, for the glycosylation of piceid. Among the different donor substrates used, the maximum transfer efficiency (TE) of glycosylation of piceid was observed for a-cyclodextrin (78.9%) followed by maltodextrin (72.1%). The partially purified piceid glycoside products (PicG(2) and PicG(3)) were identified by mass spectrometry. (C) 2011 Elsevier Ltd. All rights reserved. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Piceid, Cyclodextrin glucanotransferase, Transglycosylation, Resveratrol, Glucoside
in
Process Biochemistry
volume
47
issue
3
pages
528 - 532
publisher
Elsevier
external identifiers
  • wos:000300868700027
  • scopus:84856219989
ISSN
1873-3298
DOI
10.1016/j.procbio.2011.11.012
language
English
LU publication?
yes
id
7a601d9e-58cd-460c-a6cd-d5d3c86f196d (old id 2379196)
date added to LUP
2012-03-27 16:41:49
date last changed
2017-01-01 04:07:42
@article{7a601d9e-58cd-460c-a6cd-d5d3c86f196d,
  abstract     = {Novel glycosides of piceid (3,4'-5-trihydroxy stilbene 3-O-beta-D-glucoside) were produced by the transglycosylation reactions of cyclodextrin glucanotransferase (CGTase) from Bacillus macerans, with piceid (PicG(1)) and maltodextrin as the acceptor and donor substrates, respectively. The reactions were performed at 40 degrees C with 2.56 mM piceid (0.1% w/v) and maltodextrin (5% w/v) in 0.02 M citrate phosphate buffer, pH 6.0 containing 5% (v/v) methanol for 6h. Glucose, maltose, sucrose, maltotriose and alpha-cyclodextrin (alpha-CD) were also used to analyze their ability to function as donor substrates, for the glycosylation of piceid. Among the different donor substrates used, the maximum transfer efficiency (TE) of glycosylation of piceid was observed for a-cyclodextrin (78.9%) followed by maltodextrin (72.1%). The partially purified piceid glycoside products (PicG(2) and PicG(3)) were identified by mass spectrometry. (C) 2011 Elsevier Ltd. All rights reserved.},
  author       = {Mathew, Sindhu and Hedström, Martin and Adlercreutz, Patrick},
  issn         = {1873-3298},
  keyword      = {Piceid,Cyclodextrin glucanotransferase,Transglycosylation,Resveratrol,Glucoside},
  language     = {eng},
  number       = {3},
  pages        = {528--532},
  publisher    = {Elsevier},
  series       = {Process Biochemistry},
  title        = {Enzymatic synthesis of piceid glycosides by cyclodextrin glucanotransferase},
  url          = {http://dx.doi.org/10.1016/j.procbio.2011.11.012},
  volume       = {47},
  year         = {2012},
}