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• W2002929422 abstract "The rare sugar d-psicose is an ideal sucrose substitute for food products, due to having 70% of the relative sweetness but 0.3% of the energy of sucrose. It also shows important physiological functions. d-Tagatose 3-epimerase (DTEase) family enzymes can produce d-psicose from d-fructose. In this paper, a new member of the DTEase family of enzymes was characterized from Desmospora sp. 8437 (GenBank accession no. WP_009711885 ) and was named Desmospora sp. d-psicose 3-epimerase (DPEase) due to its highest substrate specificity toward d-psicose. Desmospora sp. DPEase was strictly metal-dependent and displayed maximum activity in the presence of Co(2+). The optimum pH and temperature were 7.5 and 60 °C, respectively. The enzyme was relatively thermostable below 50 °C, but easily lost initial activity when preincubated at 60 °C. The thermostability property was almost not affected by the addition of Co(2+). Desmospora sp. DPEase had relatively high catalysis efficiency for the substrates d-psicose and d-fructose, which were measured to be 327 and 116 mM(-1) min(-1), respectively. The equilibrium ratio between d-psicose and d-fructose of Desmospora sp. DPEase was 30:70. The enzyme could produce 142.5 g/L d-psicose from 500 g/L of d-fructose, suggesting that the enzyme is a potential d-psicose producer for industrial production." @default.
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• W2002929422 date "2013-11-15" @default.
• W2002929422 modified "2023-10-17" @default.
• W2002929422 title "Characterization of a Metal-Dependent <scp>d</scp>-Psicose 3-Epimerase from a Novel Strain, Desmospora sp. 8437" @default.
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• W2002929422 doi "https://doi.org/10.1021/jf4035817" @default.
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