Abstract
l-Xylulose was used as a raw material for the production of l-xylose with a recombinantly produced Escherichia colil-fucose isomerase as the catalyst. The enzyme had a very alkaline pH optimum (over 10.5) and displayed Michaelis–Menten kinetics for l-xylulose with a Km of 41 mM and a Vmax of 0.23 μmol/(mg min). The half-lives determined for the enzyme at 35 °C and at 45 °C were 6 h 50 min and 1 h 31 min, respectively. The reaction equilibrium between l-xylulose and l-xylose was 15:85 at 35 °C and thus favored the formation of l-xylose. Contrary to the l-rhamnose isomerase catalyzed reaction described previously [14]l-lyxose was not detected in the reaction mixture with l-fucose isomerase. Although xylitol acted as an inhibitor of the reaction, even at a high ratio of xylitol to l-xylulose the inhibition did not reach 50%.
Original language | English |
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Pages (from-to) | 71-76 |
Number of pages | 6 |
Journal | Enzyme and Microbial Technology |
Volume | 50 |
Issue number | 1 |
DOIs | |
Publication status | Published - 2012 |
MoE publication type | A1 Journal article-refereed |
Keywords
- L-Xylose
- L-Xylulose
- L-Fucose isomerase
- Isomerization
- Rare sugars