Enzymatic synthesis of piceid glycosides by cyclodextrin glucanotransferase
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/2379196
- author
- Mathew, Sindhu ; Hedström, Martin LU and Adlercreutz, Patrick LU
- organization
- publishing date
- 2012
- 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
- 2016-04-01 11:03:19
- date last changed
- 2022-03-12 19:25:23
@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}}, keywords = {{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}}, doi = {{10.1016/j.procbio.2011.11.012}}, volume = {{47}}, year = {{2012}}, }