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Article Dans Une Revue Biotechnology Journal Année : 2010

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

an G Cerdobbel
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Karel de Winter
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Tom Desmet
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Wim Soetaert
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Résumé

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 °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 °C higher than that of the soluble enzyme. Furthermore, the immobilized enzyme displays an exceptional thermostability, retaining all of its activity after one week incubation at 60 °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.

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Dates et versions

hal-00579475 , version 1 (24-03-2011)

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an G Cerdobbel, Karel de Winter, Tom Desmet, Wim Soetaert. Sucrose phosphorylase as a cross-linked enzyme aggregate: Improved thermal stability for industrial applications. Biotechnology Journal, 2010, 5 (11), pp.1192. ⟨10.1002/biot.201000202⟩. ⟨hal-00579475⟩

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