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Sucrose phosphorylase from Bifidobacterium adolescentis was recombinantly expressed in Escherichia coli and purified by use of a His-tag. Kinetic characterization of the enzyme revealed an optimal temperature for phosphorolytic activity of 58°C, which is surprisingly high for an enzyme from a mesophilic source. The temperature optimum could be further increased to 65°C by multipoint covalent immobilization...
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