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Applied and Environmental Microbiology, July 2009, p. 4705-4710, Vol. 75, No. 14
0099-2240/09/$08.00+0 doi:10.1128/AEM.00310-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Department of Bioscience and Biotechnology, Konkuk University, Seoul 143-701, Republic of Korea
Received 7 February 2009/ Accepted 11 May 2009
The uncharacterized gene previously proposed as a mannose-6-phosphate isomerase from Bacillus subtilis was cloned and expressed in Escherichia coli. The maximal activity of the recombinant enzyme was observed at pH 7.5 and 40°C in the presence of 0.5 mM Co2+. The isomerization activity was specific for aldose substrates possessing hydroxyl groups oriented in the same direction at the C-2 and C-3 positions, such as the D and L forms of ribose, lyxose, talose, mannose, and allose. The enzyme exhibited the highest activity for L-ribulose among all pentoses and hexoses. Thus, L-ribose, as a potential starting material for many L-nucleoside-based pharmaceutical compounds, was produced at 213 g/liter from 300-g/liter L-ribulose by mannose-6-phosphate isomerase at 40°C for 3 h, with a conversion yield of 71% and a volumetric productivity of 71 g liter–1 h–1.
Published ahead of print on 15 May 2009.
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