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• W2106890918 abstract "ABSTRACT Enzymatic processes are useful for industrially important sugar production, and in vitro two-step isomerization has proven to be an efficient process in utilizing readily available sugar sources. A hypothetical uncharacterized protein encoded by ydaE of Bacillus licheniformis was found to have broad substrate specificities and has shown high catalytic efficiency on d -lyxose, suggesting that the enzyme is d -lyxose isomerase. Escherichia coli BL21 expressing the recombinant protein, of 19.5 kDa, showed higher activity at 40 to 45°C and pH 7.5 to 8.0 in the presence of 1.0 mM Mn 2+ . The apparent K m values for d -lyxose and d -mannose were 30.4 ± 0.7 mM and 26 ± 0.8 mM, respectively. The catalytic efficiency ( k cat / K m ) for lyxose (3.2 ± 0.1 mM −1 s −1 ) was higher than that for d -mannose (1.6 mM −1 s −1 ). The purified protein was applied to the bioproduction of d -lyxose and d -glucose from d -xylose and d -mannose, respectively, along with the thermostable xylose isomerase of Thermus thermophilus HB08. From an initial concentration of 10 mM d -lyxose and d -mannose, 3.7 mM and 3.8 mM d -lyxose and d -glucose, respectively, were produced by two-step isomerization. This two-step isomerization is an easy method for in vitro catalysis and can be applied to industrial production." @default.
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• W2106890918 date "2011-05-15" @default.
• W2106890918 modified "2023-10-14" @default.
• W2106890918 title "Substrate Specificity of the Bacillus licheniformis Lyxose Isomerase YdaE and Its Application in <i>In Vitro</i> Catalysis for Bioproduction of Lyxose and Glucose by Two-Step Isomerization" @default.
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• W2106890918 doi "https://doi.org/10.1128/aem.02693-10" @default.
• W2106890918 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3126444" @default.
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