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Characterization of a recombinant l-rhamnose isomerase from Dictyoglomus turgidum and its application for l-rhamnulose production

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Abstract

A putative recombinant enzyme from Dictyoglomus turgidum was characterized and immobilized on Duolite A568 beads. The native enzyme was a 46 kDa tetramer. Its activity was highest for l-rhamnose, indicating that it is an l-rhamnose isomerase. The maximum activities of both the free and immobilized enzymes for l-rhamnose isomerization were at pH 8.0 and 75 °C in the presence of Mn2+. Under these conditions, the half-lives of the free and immobilized enzymes were 28 and 112 h, respectively. In a packed-bed bioreactor, the immobilized enzyme produced an average of 130 g l-rhamnulose l−1 from 300 g l-rhamnose l−1 after 240 h at pH 8.0, 70 °C, and 0.6 h−1, with a productivity of 78 g l−1 h−1 and a conversion yield of 43 %. To the best of our knowledge, this is the first report describing the enzymatic production of l-rhamnulose.

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Acknowledgments

This work was supported by the Basic Research Lab program (No. 2010-0019306), the National Research Foundation, the Ministry of Education, Science and Technology, Republic of Korea.

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Correspondence to Deok-Kun Oh.

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Kim, YS., Shin, KC., Lim, YR. et al. Characterization of a recombinant l-rhamnose isomerase from Dictyoglomus turgidum and its application for l-rhamnulose production. Biotechnol Lett 35, 259–264 (2013). https://doi.org/10.1007/s10529-012-1069-2

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  • DOI: https://doi.org/10.1007/s10529-012-1069-2

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