Novel Substrate Specificity of D-Arabinose Isomerase from Klebsiella pneumoniae and Its Application to Production of D-Altrose from D-Psicose(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)

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D-Arabinose isomerase from Klebsiella pneumoniae 40bXX was purified 12-fold with a 62.5% yield indicated by its electrophoretic homogeneity. The purified enzyme showed the highest activities toward D-arabinose and L-fucose as substrates at optimum conditions (50mM glycine-NaOH, pH 9.0, 40℃). The enzyme had a broad range of substrate specificities toward various D/L-aldoses, i.e., D-arabinose, L-fucose, D/L-xylose, D-mannose, D/L-lyxose, L-glucose, D-altrose and D/L-galactose. The equilibrium ratios between D-arabinose and D-ribulose, L-fucose and L-fuculose, D-altrose and D-psicose, and L-galactose and L-tagatose were 90:10, 90:10, 13:87 and 25:75, respectively. Using a combination of the immobilized D-tagatose 3-epimerase and D-arabinose isomerase, we achieved the production of D-altrose from D-fructose in a batch reactor. We successfully produced approximately 12g of D-altrose from 200g of D-fructose in a reaction series with an overall yield of 6%. The product obtained was confirmed to be D-altrose by HPLC and ^<13>C-NMR. To the best of our knowledge, this is the first report on the production of D-altrose from a cheap sugar, D-fructose, using an enzymatic method.
社団法人日本生物工学会の論文
2006-11-25