Abstract
d-Psicose was produced from d-fructose using an immobilized d-tagatose 3-epimerase ( d-TE), and used as a substrate for the production of d-allose by immobilized l-rhamnose isomerase ( l-RI). d-Allose was produced from d-ssicose by l-RI, which was constitutively produced by a mutant strain of Pseudomonas sp. LL172 and immobilized on chitopearl beads of BCW 2603. The isomerization reaction progressed steadily while the concentration of d-psicose was increased from 2.5 to 20% in Tris-HCl buffer (0.05 M, pH 7.5), and about 40% of d-psicose was converted to d-allose in all the cases. The immobilized enzyme was stable even after repeated use over 20 d at 40°C in the preparation of d-allose without detectable decrease in the enzyme activity, indicating the high stability of the enzyme in the batch reaction. The crystallized product was confirmed as d-allose by analysis of the IR spectra, NMR spectra, melting point and optical rotation.
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