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

An Cerdobbel (UGent), Karel De Winter, Tom Desmet (UGent) and Wim Soetaert (UGent)
(2010) BIOTECHNOLOGY JOURNAL. 5(11). p.1192-1197
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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.
Keywords
Cross-linked enzyme aggregate, Sucrose phosphorylase, Thermostability, Enzyme immobilization, ASSAY, Biocatalysis, LEUCONOSTOC-MESENTEROIDES, CRYSTALS, THERMOZYMES, IMMOBILIZED ENZYMES, PENICILLIN ACYLASE, ESCHERICHIA-COLI, GLUCOSE, LINKING

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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.
@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},
}

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