Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Synthesis of novel oligomeric anionic alkyl glycosides using laccase/TEMPO oxidation and cyclodextrin glucanotransferase (CGTase)‐catalysed transglycosylation

Ngo, Ngoc T. N. LU ; Linares-Pastén, Javier A. LU orcid ; Grey, Carl LU orcid and Adlercreutz, Patrick LU orcid (2021) In Biotechnology and Bioengineering 118(7). p.2548-2558
Abstract
Modification of alkyl glycosides, to alter their properties and widen the scope of potential applications, is of considerable interest. Here, we report the synthesis of new anionic alkyl glycosides with long carbohydrate chains, using two different approaches: laccase/TEMPO oxidation of a long‐carbohydrate‐chain alkyl glycoside, and cyclodextrin glucanotransferase (CGTase)‐catalysed elongation of anionic alkyl glycosides. The laccase/TEMPO oxidation of dodecyl β‐D‐maltooctaoside proceeded efficiently with the formation of aldehyde and acid products. However, depolymerization occurred to a large extent, limiting the product yield and purity. On the other hand, CGTase‐catalysed coupling/disproportionation reactions with α‐cyclodextrin and... (More)
Modification of alkyl glycosides, to alter their properties and widen the scope of potential applications, is of considerable interest. Here, we report the synthesis of new anionic alkyl glycosides with long carbohydrate chains, using two different approaches: laccase/TEMPO oxidation of a long‐carbohydrate‐chain alkyl glycoside, and cyclodextrin glucanotransferase (CGTase)‐catalysed elongation of anionic alkyl glycosides. The laccase/TEMPO oxidation of dodecyl β‐D‐maltooctaoside proceeded efficiently with the formation of aldehyde and acid products. However, depolymerization occurred to a large extent, limiting the product yield and purity. On the other hand, CGTase‐catalysed coupling/disproportionation reactions with α‐cyclodextrin and dodecyl β‐D‐maltoside diuronic acid (DDM‐2COOH) or octyl β‐D‐glucuronic acid (OG‐COOH) as substrates gave high conversions, especially when the CGTase Toruzyme was used. It was found that pH had a strong influence on both the enzyme activity and the acceptor specificity. With non‐ionic substrates (dodecyl β‐D‐maltoside and octyl β‐D‐glucoside), Toruzyme exhibited high catalytic activity at pH 5‐6, but for the acidic substrates (DDM‐2COOH and OG‐COOH) the activity was highest at pH 4. This is most likely due to the enzyme favoring the protonated forms of DDM‐2COOH and OG‐COOH, which exist at lower pH (pKa about 3). (Less)
Please use this url to cite or link to this publication:
author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Octyl β-D-glucoside, Octyl β-D-glucuronic acid, Dodecyl β-D-maltoside, Dodecyl β-D-maltoside diuronic acid, Oxidation, Laccase, TEMPO, Cyclodextrin glucanotransferase (CGTase), Toruzyme 3.0L
in
Biotechnology and Bioengineering
volume
118
issue
7
pages
11 pages
publisher
John Wiley & Sons Inc.
external identifiers
  • scopus:85104511172
  • pmid:33788276
ISSN
1097-0290
DOI
10.1002/bit.27770
language
English
LU publication?
yes
id
9fe9524a-8bb2-41b6-a062-903ca469a94a
date added to LUP
2021-04-08 19:17:33
date last changed
2024-10-05 21:30:34
@article{9fe9524a-8bb2-41b6-a062-903ca469a94a,
  abstract     = {{Modification of alkyl glycosides, to alter their properties and widen the scope of potential applications, is of considerable interest. Here, we report the synthesis of new anionic alkyl glycosides with long carbohydrate chains, using two different approaches: laccase/TEMPO oxidation of a long‐carbohydrate‐chain alkyl glycoside, and cyclodextrin glucanotransferase (CGTase)‐catalysed elongation of anionic alkyl glycosides. The laccase/TEMPO oxidation of dodecyl β‐D‐maltooctaoside proceeded efficiently with the formation of aldehyde and acid products. However, depolymerization occurred to a large extent, limiting the product yield and purity. On the other hand, CGTase‐catalysed coupling/disproportionation reactions with α‐cyclodextrin and dodecyl β‐D‐maltoside diuronic acid (DDM‐2COOH) or octyl β‐D‐glucuronic acid (OG‐COOH) as substrates gave high conversions, especially when the CGTase Toruzyme was used. It was found that pH had a strong influence on both the enzyme activity and the acceptor specificity. With non‐ionic substrates (dodecyl β‐D‐maltoside and octyl β‐D‐glucoside), Toruzyme exhibited high catalytic activity at pH 5‐6, but for the acidic substrates (DDM‐2COOH and OG‐COOH) the activity was highest at pH 4. This is most likely due to the enzyme favoring the protonated forms of DDM‐2COOH and OG‐COOH, which exist at lower pH (pKa about 3).}},
  author       = {{Ngo, Ngoc T. N. and Linares-Pastén, Javier A. and Grey, Carl and Adlercreutz, Patrick}},
  issn         = {{1097-0290}},
  keywords     = {{Octyl β-D-glucoside; Octyl β-D-glucuronic acid; Dodecyl β-D-maltoside; Dodecyl β-D-maltoside diuronic acid; Oxidation; Laccase; TEMPO; Cyclodextrin  glucanotransferase (CGTase); Toruzyme 3.0L}},
  language     = {{eng}},
  month        = {{07}},
  number       = {{7}},
  pages        = {{2548--2558}},
  publisher    = {{John Wiley & Sons Inc.}},
  series       = {{Biotechnology and Bioengineering}},
  title        = {{Synthesis of novel oligomeric anionic alkyl glycosides using laccase/TEMPO oxidation and cyclodextrin glucanotransferase (CGTase)‐catalysed transglycosylation}},
  url          = {{http://dx.doi.org/10.1002/bit.27770}},
  doi          = {{10.1002/bit.27770}},
  volume       = {{118}},
  year         = {{2021}},
}