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The d-psicose 3-epimerase (DPE) gene from Ruminococcus sp. was cloned and overexpressed in Escherichia coli. The recombinant protein was purified and characterized. It was optimally active at pH 7.5–8.0 and 60 °C. Activity was not dependent on the presence of metal ions; however, it became more thermostable with added Mn2+. The Km of the enzyme for d-psicose (48 mM) was lower than that for d-tagatose...
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