Improvements of enzyme activity and enantioselectivity in lipase-catalyzed alcoholysis of (R,S)-azolides

An Chi Wu, Pei Yun Wang, Yi Sheng Lin, Min Fang Kao, Jin Ru Chen, Jyun Fen Ciou, Shau Wei Tsai*

*此作品的通信作者

研究成果: 期刊稿件文章同行評審

25 引文 斯高帕斯(Scopus)

摘要

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)=0.979mmol/(hg) were greatly improved in comparison with VR/VS=8.0 and VR/(Et)=0.113mmol/(hg) 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.

原文英語
頁(從 - 到)235-241
頁數7
期刊Journal of Molecular Catalysis B: Enzymatic
62
發行號3-4
DOIs
出版狀態已出版 - 2010

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