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 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%.
- L-Fucose isomerase
- Rare sugars
Usvalampi, A., Turunen, O., Valjakka, J., Pastinen, O., Leisola, M., & Nyyssölä, A. (2012). Production of l-xylose from l-xylulose using Escherichia coli l-fucose isomerase. Enzyme and Microbial Technology, 50(1), 71-76. https://doi.org/10.1016/j.enzmictec.2011.09.009