Biotechnology Letters

, Volume 32, Issue 2, pp 299–304

Characterization of a recombinant l-fucose isomerase from Caldicellulosiruptor saccharolyticus that isomerizes l-fucose, d-arabinose, d-altrose, and l-galactose

Authors

  • Yo-Han Ju
    • Department of Bioscience and BiotechnologyKonkuk University
    • Department of Bioscience and BiotechnologyKonkuk University
Original Research Paper

DOI: 10.1007/s10529-009-0154-7

Cite this article as:
Ju, Y. & Oh, D. Biotechnol Lett (2010) 32: 299. doi:10.1007/s10529-009-0154-7

Abstract

A recombinant l-fucose isomerase from Caldicellulosiruptor saccharolyticus was purified as a single 68 kDa band with an activity of 76 U mg−1. The molecular mass of the native enzyme was 204 kDa as a trimer. The maximum activity for l-fucose isomerization was at pH 7 and 75°C in the presence of 1 mM Mn2+. Its half-life at 70°C was 6.1 h. For aldose substrates, the enzyme displayed activity in decreasing order for l-fucose, with a kcat of 11,910 min−1 and a Km of 140 mM, d-arabinose, d-altrose, and l-galactose. These aldoses were converted to the ketoses l-fuculose, d-ribulose, d-psicose, and l-tagatose, respectively, with 24, 24, 85, 55% conversion yields after 3 h.

Keywords

l-ArabinoseCaldicellulosiruptor saccharolyticusl-Fucosel-Fucose isomeraseSugar isomeraseThermostable enzyme

Copyright information

© Springer Science+Business Media B.V. 2009