Optimizing the Enzymatic Kinetic Resolution of(R/S)-δ-Tetradecalactone by Response Surface Methodology
A series of lipases were screened using δ-tetradecalactone as substrate by pre-column derivatization HPLC analysis.Aspergillus niger lipase(ANL)and Pseudomonas cepacia lipase(PCL)with specific hydrolysis substrate of(R/S)-5-hydroxytetradecanoic acid were obtained.The effects of pH,temperature,cosolvent,enzyme-ester ratio and reaction time on the optical purity(eep)and yield(Y)of the product were investigated.The optimum reaction conditions were determined by response surface analysis(CCD).After optimization,(S)-5-hydroxytetradecanoic acid(eep1≥99.9%,yield 42.0%)and(R)-5-hydroxytetradecanoic acid(eep2≥99.9%,yield 49.0%)were obtained.The system meets the requirements of green chemistry and has good application potential.
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