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• W2084310240 startingPage "235" @default.
• W2084310240 abstract "With Candida antarctica lipase B (CALB)-catalyzed alcoholysis of (R,S)-naproxenyl 1,2,4-triazolide at the optimal conditions (i.e. anhydrous MTBE as the solvent, and methanol as the acyl acceptor at 45 °C) as the model system, the enzyme enantioselectivity in terms of VR/VS = 105.8 and specific activity for the fast-reacting (R)-azolide VR/(Et) = 0.979 mmol/(h g) were greatly improved in comparison with VR/VS = 8.0 and VR/(Et) = 0.113 mmol/(h g) of using (R,S)-naproxenyl 2,2,2-trifluoroethyl ester as the substrate. The resolution strategy was successfully extended to other (R,S)-profenyl 1,2,4-triazolides and lipases from Candida rugosa (Lipase MY) and Carica papaya (CPL) having opposite enantioselectivity to CALB. Moreover, the kinetic constants were estimated, compared with those obtained via hydrolysis, and employed for modeling time-course conversions of (R,S)-naproxenyl 1,2,4-triazolide in anhydrous MTBE. The advantages of easy substrate preparation, high enzyme reactivity and enantioselectivity, as well as easy product separation from the remaining substrate via reactive extraction demonstrate merits of using (R,S)-azolides but not the corresponding esters for the alcoholytic resolution." @default.
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• W2084310240 date "2010-03-01" @default.
• W2084310240 modified "2023-10-07" @default.
• W2084310240 title "Improvements of enzyme activity and enantioselectivity in lipase-catalyzed alcoholysis of (R,S)-azolides" @default.
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• W2084310240 doi "https://doi.org/10.1016/j.molcatb.2009.11.001" @default.
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