The BaM6PI gene encoding a mannose-6-phosphate isomerase (M6PI, EC 5.3.1.8) was cloned from Bacillus amyloliquefaciens DSM7 and overexpressed in Escherichia coli. The enzyme activity of BaM6PI was optimal at pH and temperature of 7.5 and 70°C, respectively, with a kcat/Km of 13,900 s-1 mM-1 for mannose-6-phosphate (M6P). The purified BaM6PI demonstrated the highest catalytic efficiency of all characterized M6PIs. Although M6PIs have been characterized from several other sources, BaM6PI is distinguished from other M6PIs by its wide pH range and high catalytic efficiency for M6P. The binding orientation of the substrate M6P in the active site of BaM6PI shed light on the molecular basis of its unusually high activity. BaM6PI showed 97% substrate conversion from M6P to fructose-6-phosphate demonstrating the potential for using BaM6PI in industrial applications.
The liquid–liquid equilibria for the water + n-pentanoic acid + n-heptane system and the water + n-pentanoic acid + dichloromethane system were determined at 298.2 K. The NRTL and UNIQUAC models were applied to both ternary systems. The interaction parameters obtained from the NRTL model correlated with the equilibrium compositions better than those from the UNIQUAC model.
The liquid−liquid equilibria for water + 3-methyl-2-cyclopentenone + ethyl acetate and water + 3-methyl-2-cyclopentenone + methyl tert-butyl ether system were determined at 293.2 K. The NRTL and UNIQUAC
models were applied to both ternary systems. The interaction parameters obtained from both models
successfully correlated the equilibrium compositions.
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