1239618-86-0Relevant academic research and scientific papers
Lipase-catalyzed kinetic resolution of 2-methylene-substituted cycloalkanols in batch and continuous-flow modes
Tomin, Anna,Hornyánszky, Gábor,Kupai, Katalin,Dorkó, Zsanett,ürge, László,Darvas, Ferenc,Poppe, László
experimental part, p. 859 - 865 (2011/12/15)
Kinetic resolutions of cyclic racemic secondary alcohols (2-methylenecyclopentan-1-ol rac-1a, 2-methylenecyclohexan-1-ol rac-1b, 2-methylenecycloheptan-1-ol rac-1c, 6-methylene-[1,3]dioxepan-5-ol rac-1d, 2,2-dimethyl-6-methylene-[1,3]dioxepan-5-ol rac-1e and trans-2-bromocyclohexan-1-ol rac-3) catalyzed by different (commercial and in-house-made) lipases were performed using vinyl acetate in THF-hexane. In the most typical cases (rac-1b, rac-1d and rac-3), the immobilized Candida antarctica lipase B (CaLB, for rac-1b and rac-3)- or sol-gel immobilized Pseudomonas fluorescens lipase (sol-gel LAK, for rac-1d)-catalyzed batch mode reactions were compared to the continuous mode reactions carried out in an enzyme-filled stainless steel bioreactor. The effect of temperature (20-60 °C) and flow rate (0.1-0.3 ml min-1) on the continuous-flow acetylation of rac-1b, rac-1d and rac-3 were investigated. In the kinetic resolutions of rac-1b, rac-1d and rac-3, the enantiomeric selectivities (E) were similar in the continuous-flow and batch (shake flask) modes. However, the productivities (specific reaction rate: r), were significantly higher in the continuous-flow mode biotransformations of rac-1b, rac-1d and rac-3.
