Purification and Characterization of Sucrose Phosphorylase from Leuconostoc mesenteroides ATCC 12291 Cells, and Disaccharides Synthesis by the Enzyme

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A sucrose phosphorylase was purified from Leuconostoc mesenteroides ATCC 12291 cells to an electrophoretically homogeneous state with hydrophobic, ion-exchange and gel filtration column chromatographies. The enzyme had a molecular weight of 55, 000 and pI of 4.0. It showed the maximum activity at pH 6.5 in a transfer reaction of glucose residue from a-D-glucose -l-phosphate (G-1-P), at pH 7.0 in a transfer reaction from sucrose and is fully stable at pH between 5.5 and 7.5. It showed the maximum activity at 35°C and is stable below 40°C. D-Fructose, D-xylulose, L-arabinose, Lsorbose and L-ribulose can serve as an acceptor in the transfer reaction from G-1-P, and the last four can serve as an acceptor in the reaction from sucrose, too. It was found that the reactions with sucrose gave a higher yield than those with G-1-P . Among the reactions tested, glucosylxyluloside synthesis from sucrose and xylulose gave the highest yield.
日本応用糖質科学会の論文