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Sucrose phosphorylase as cross-linked enzyme aggregate: improved thermal stability for industrial applications

An Cerdobbel UGent, Karel De Winter UGent, Tom Desmet UGent and Wim Soetaert UGent (2010) BIOTECHNOLOGY JOURNAL. 5(11). p.1192-1197
abstract
Sucrose phosphorylase is an interesting biocatalyst that can glycosylate a variety of small molecules using sucrose as a cheap but efficient donor substrate. The low thermostability of the enzyme, however, limits its industrial applications, as these are preferably performed at 60 degrees C to avoid microbial contamination. Cross-linked enzyme aggregates (CLEAs) of the sucrose phosphorylase from Bifidobacterium adolescentis were found to have a temperature optimum that is 17 degrees C higher than that of the soluble enzyme. Furthermore, the immobilized enzyme displays an exceptional thermostability, retaining all of its activity after 1 week incubation at 60 degrees C. Recycling of the biocatalyst allows its use in at least ten consecutive reactions, which should dramatically increase the commercial potential of its glycosylating activity.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
Cross-linked enzyme aggregate, Sucrose phosphorylase, Thermostability, Enzyme immobilization, ASSAY, Biocatalysis, LEUCONOSTOC-MESENTEROIDES, CRYSTALS, THERMOZYMES, IMMOBILIZED ENZYMES, PENICILLIN ACYLASE, ESCHERICHIA-COLI, GLUCOSE, LINKING
journal title
BIOTECHNOLOGY JOURNAL
Biotechnol. J.
volume
5
issue
11
pages
1192 - 1197
Web of Science type
Article
Web of Science id
000284012300018
ISSN
1860-6768
DOI
10.1002/biot.201000202
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
1088621
handle
http://hdl.handle.net/1854/LU-1088621
date created
2010-12-16 16:34:18
date last changed
2011-03-23 13:14:20
@article{1088621,
  abstract     = {Sucrose phosphorylase is an interesting biocatalyst that can glycosylate a variety of small molecules using sucrose as a cheap but efficient donor substrate. The low thermostability of the enzyme, however, limits its industrial applications, as these are preferably performed at 60 degrees C to avoid microbial contamination. Cross-linked enzyme aggregates (CLEAs) of the sucrose phosphorylase from Bifidobacterium adolescentis were found to have a temperature optimum that is 17 degrees C higher than that of the soluble enzyme. Furthermore, the immobilized enzyme displays an exceptional thermostability, retaining all of its activity after 1 week incubation at 60 degrees C. Recycling of the biocatalyst allows its use in at least ten consecutive reactions, which should dramatically increase the commercial potential of its glycosylating activity.},
  author       = {Cerdobbel, An and De Winter, Karel and Desmet, Tom and Soetaert, Wim},
  issn         = {1860-6768},
  journal      = {BIOTECHNOLOGY JOURNAL},
  keyword      = {Cross-linked enzyme aggregate,Sucrose phosphorylase,Thermostability,Enzyme immobilization,ASSAY,Biocatalysis,LEUCONOSTOC-MESENTEROIDES,CRYSTALS,THERMOZYMES,IMMOBILIZED ENZYMES,PENICILLIN ACYLASE,ESCHERICHIA-COLI,GLUCOSE,LINKING},
  language     = {eng},
  number       = {11},
  pages        = {1192--1197},
  title        = {Sucrose phosphorylase as cross-linked enzyme aggregate: improved thermal stability for industrial applications},
  url          = {http://dx.doi.org/10.1002/biot.201000202},
  volume       = {5},
  year         = {2010},
}

Chicago
Cerdobbel, An, Karel De Winter, Tom Desmet, and Wim Soetaert. 2010. “Sucrose Phosphorylase as Cross-linked Enzyme Aggregate: Improved Thermal Stability for Industrial Applications.” Biotechnology Journal 5 (11): 1192–1197.
APA
Cerdobbel, A., De Winter, K., Desmet, T., & Soetaert, W. (2010). Sucrose phosphorylase as cross-linked enzyme aggregate: improved thermal stability for industrial applications. BIOTECHNOLOGY JOURNAL, 5(11), 1192–1197.
Vancouver
1.
Cerdobbel A, De Winter K, Desmet T, Soetaert W. Sucrose phosphorylase as cross-linked enzyme aggregate: improved thermal stability for industrial applications. BIOTECHNOLOGY JOURNAL. 2010;5(11):1192–7.
MLA
Cerdobbel, An, Karel De Winter, Tom Desmet, et al. “Sucrose Phosphorylase as Cross-linked Enzyme Aggregate: Improved Thermal Stability for Industrial Applications.” BIOTECHNOLOGY JOURNAL 5.11 (2010): 1192–1197. Print.