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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

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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 Mn2+, 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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Acknowledgments

This work was supported by the Korea Science and Engineering Foundation (KOSEF) through the National Research Lab. Program funded by the Ministry of Education, Science and Technology (R0A-2007-000-20015-0) and by a grant (Code #2007-0301034024) from BioGreen 21 Program, Rural Development Administration.

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Correspondence to Deok-Kun Oh.

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Park, CS., Yeom, SJ., Lim, YR. et al. 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. Biotechnol Lett 32, 1947–1953 (2010). https://doi.org/10.1007/s10529-010-0385-7

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  • DOI: https://doi.org/10.1007/s10529-010-0385-7

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