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  • Title: Characterization of a recombinant thermostable L: -rhamnose isomerase from Thermotoga maritima ATCC 43589 and its application in the production of L-lyxose and L-mannose.
    Author: Park CS, Yeom SJ, Lim YR, Kim YS, Oh DK.
    Journal: Biotechnol Lett; 2010 Dec; 32(12):1947-53. PubMed ID: 20809285.
    Abstract:
    A putative L-rhamnose isomerase (RhaA) from Thermotoga maritima was purified with a specific activity of 55 U/mg by His-Trap affinity chromatography. The native enzyme was estimated as a 46 kDa tetramer by gel filtration chromatography. The half-lives of the enzyme at 75, 80, 85, 90 and 95°C were 773, 347, 187, 118, and 65 h, respectively, indicating that it is the most thermostable of all RhaAs. Under the optimum conditions of pH 8.0, 85°C, and 1 mM Mn(2+), RhaA with 100 U enzyme/ml converted 500 L-xylulose/l to 225 g/l L-lyxose after 3 h, and converted 500 L-fructose/l to 175 g/l L-mannose after 5 h.
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