Novel substrate specificity of D-arabinose isomerase from Klebsiella pneumoniae and its application to production of D-altrose from D-psicose
2006
Menavuvu, B.T.(Kagawa Univ., Miki (Japan). Faculty of Agriculture and Rare Sugar Research Center) | Poonperm, W. | Takeda, K. | Morimoto, K. | Granstroem, T.B. | Takada, G. | Izumori, K.
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 (50 mM glycine NaOH, pH 9.0, 40 deg C). The enzyme had a broad range of substrate specificities toward various D/L-aldoses, i.e., D-arabinose, L-fucose, D/L-xyiose, 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 12 g of D-altrose from 200 g 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 sup(13)CNMR. 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.
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