Abstract
l-Xylulose was used as a raw material for the production of l-xylose with a recombinantly produced Escherichia coli l-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 K m of 41mM and a V max of 0.23μmol/(mgmin). The half-lives determined for the enzyme at 35°C and at 45°C were 6h 50min and 1h 31min, 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 |
|---|---|
| Pages (from-to) | 71-76 |
| Number of pages | 6 |
| Journal | Enzyme and Microbial Technology |
| Volume | 50 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 2012 |
| Publication type | A1 Journal article-refereed |
Keywords
- Isomerization
- L-Fucose isomerase
- L-Xylose
- L-Xylulose
- Rare sugars
- l-Fucose isomerase
- l-Xylose
- l-Xylulose
Publication forum classification
- Publication forum level 1
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