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Characterization of a recombinant thermostable d-lyxose isomerase from Dictyoglomus turgidum that produces d-lyxose from d-xylulose

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Abstract

A putative d-lyxose isomerase from Dictyoglomus turgidum was purified with a specific activity of 19 U/mg for d-lyxose isomerization by heat treatment and affinity chromatography. The native enzyme was estimated as a 42 kDa dimer by gel-filtration chromatography. The activity of the enzyme was highest for d-lyxose, suggesting that it is a d-lyxose isomerase. The maximum activity of the enzyme was at pH 7.5 and 75°C in the presence of 0.5 mM Co2+, with a half-life of 108 min, K m of 39 mM, and k cat of 3,570 1/min. The enzyme is the most thermostable d-lyxose isomerase among those characterized to date. It converted 500 g d-xylulose/l to 380 g d-lyxose/l after 2 h. This is the highest concentration and productivity of d-lyxose reported thus far.

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Acknowledgment

This work was supported by Konkuk University in 2011.

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Correspondence to Deok-Kun Oh.

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Choi, JG., Hong, SH., Kim, YS. et al. Characterization of a recombinant thermostable d-lyxose isomerase from Dictyoglomus turgidum that produces d-lyxose from d-xylulose. Biotechnol Lett 34, 1079–1085 (2012). https://doi.org/10.1007/s10529-012-0874-y

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  • DOI: https://doi.org/10.1007/s10529-012-0874-y

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