Abstract
A non-characterized gene, previously proposed as the d-tagatose-3-epimerase gene from Rhodobacter sphaeroides, was cloned and expressed in Escherichia coli. Its molecular mass was estimated to be 64 kDa with two identical subunits. The enzyme specificity was highest with d-fructose and decreased for other substrates in the order: d-tagatose, d-psicose, d-ribulose, d-xylulose and d-sorbose. Its activity was maximal at pH 9 and 40°C while being enhanced by Mn2+. At pH 9 and 40°C, 118 g d-psicose l−1 was produced from 700 g d-fructose l−1 after 3 h.
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Acknowledgements
This research was supported financially by the National High Technology Research and Development Program of People’s Republic of China (2006AA10Z334) as well as the Research Program of State Key Laboratory of Food Science and Technology, Jiangnan University (SKLF-MB-200804 and SKLF-TS-200805).
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Supplementary Fig. 1
SDS-PAGE of purified R. sphaeroides d-tagatose-3-epimerase. Lane 1, molecular mass markers (kDa); lane 2, purified R. sphaeroides d-tagatose-3-epimerase (DOC 276 kb)
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Zhang, L., Mu, W., Jiang, B. et al. Characterization of d-tagatose-3-epimerase from Rhodobacter sphaeroides that converts d-fructose into d-psicose. Biotechnol Lett 31, 857–862 (2009). https://doi.org/10.1007/s10529-009-9942-3
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DOI: https://doi.org/10.1007/s10529-009-9942-3