title: Sucrose phosphorylase as cross-linked enzyme aggregate: improved thermal stability for industrial applications.
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°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 1 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.
authors.affiliation: Department of Biochemical and Microbial Technology, Ghent University, Ghent, Belgium. an.cerdobbel@ugent.be
authors.forename: An
authors.initials: A
authors.lastname: Cerdobbel
authors.forename: Karel
authors.initials: K
authors.lastname: De Winter
authors.forename: Tom
authors.initials: T
authors.lastname: Desmet
authors.forename: Wim
authors.initials: W
authors.lastname: Soetaert
mesh_terms: D001644:Bifidobacterium / Q000201:enzymology; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry* / Q000378:metabolism*; D005964:Glucosyltransferases / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D004800:Enzymes, Immobilized; D005964:Glucosyltransferases; C025901:sucrose phosphorylase