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Preparation and use of sucrose phosphorylase as cross-linked enzyme aggregate (CLEA)

Karel De Winter, Tom Desmet UGent, An Cerdobbel UGent and Wim Soetaert UGent (2012) Practical methods for biocatalysis and biotransformations 2. p.240-244
abstract
Sucrose phosphorylase (SP) can be used for the production of α-D-glucose-1-phosphate (α-G1P) by the phosphorolysis of sucrose into α-G1P and fructose. Moreover, a variety of glycosylated compounds can be produced with this enzyme, thanks to its broad acceptor specificity. Unfortunately, the use of SP at industrial scale is hampered by the lack of thermostable enzyme variants. We have recently found, however, that the stability of the SP from Bifidobacterium adolescentis can be dramatically improved by immobilization, either by covalent coupling to a Sepabeads carrier or by forming cross-linked enzyme aggregates (CLEAs).
Please use this url to cite or link to this publication:
author
organization
year
type
bookChapter
publication status
published
subject
keyword
Sucrose phosphorylase, α-D-glucose-1-phosphate, Production, CLEAs
book title
Practical methods for biocatalysis and biotransformations 2
editor
John Whittall and Peter W Sutton
pages
240 - 244
publisher
Wiley
place of publication
Chichester, UK
ISBN
9781119943426
9781119991397
DOI
10.1002/9781119943426.ch9
language
English
UGent publication?
yes
classification
B2
copyright statement
I have transferred the copyright for this publication to the publisher
id
2119158
handle
http://hdl.handle.net/1854/LU-2119158
date created
2012-05-30 09:12:02
date last changed
2017-01-02 09:54:42
@incollection{2119158,
  abstract     = {Sucrose phosphorylase (SP) can be used for the production of \ensuremath{\alpha}-D-glucose-1-phosphate (\ensuremath{\alpha}-G1P) by the phosphorolysis of sucrose into \ensuremath{\alpha}-G1P and fructose. Moreover, a variety of glycosylated compounds can be produced with this enzyme, thanks to its broad acceptor specificity. Unfortunately, the use of SP at industrial scale is hampered by the lack of thermostable enzyme variants. We have recently found, however, that the stability of the SP from Bifidobacterium adolescentis can be dramatically improved by immobilization, either by covalent coupling to a Sepabeads carrier or by forming cross-linked enzyme aggregates (CLEAs).},
  author       = {De Winter, Karel and Desmet, Tom and Cerdobbel, An and Soetaert, Wim},
  booktitle    = {Practical methods for biocatalysis and biotransformations 2},
  editor       = {Whittall, John and Sutton, Peter W},
  isbn         = {9781119943426},
  keyword      = {Sucrose phosphorylase,\ensuremath{\alpha}-D-glucose-1-phosphate,Production,CLEAs},
  language     = {eng},
  pages        = {240--244},
  publisher    = {Wiley},
  title        = {Preparation and use of sucrose phosphorylase as cross-linked enzyme aggregate (CLEA)},
  url          = {http://dx.doi.org/10.1002/9781119943426.ch9},
  year         = {2012},
}

Chicago
De Winter, Karel, Tom Desmet, An Cerdobbel, and Wim Soetaert. 2012. “Preparation and Use of Sucrose Phosphorylase as Cross-linked Enzyme Aggregate (CLEA).” In Practical Methods for Biocatalysis and Biotransformations 2, ed. John Whittall and Peter W Sutton, 240–244. Chichester, UK: Wiley.
APA
De Winter, K., Desmet, T., Cerdobbel, A., & Soetaert, W. (2012). Preparation and use of sucrose phosphorylase as cross-linked enzyme aggregate (CLEA). In J. Whittall & P. W. Sutton (Eds.), Practical methods for biocatalysis and biotransformations 2 (pp. 240–244). Chichester, UK: Wiley.
Vancouver
1.
De Winter K, Desmet T, Cerdobbel A, Soetaert W. Preparation and use of sucrose phosphorylase as cross-linked enzyme aggregate (CLEA). In: Whittall J, Sutton PW, editors. Practical methods for biocatalysis and biotransformations 2. Chichester, UK: Wiley; 2012. p. 240–4.
MLA
De Winter, Karel, Tom Desmet, An Cerdobbel, et al. “Preparation and Use of Sucrose Phosphorylase as Cross-linked Enzyme Aggregate (CLEA).” Practical Methods for Biocatalysis and Biotransformations 2. Ed. John Whittall & Peter W Sutton. Chichester, UK: Wiley, 2012. 240–244. Print.