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Rizzi, M., Stylos, P. and Reuss, M. (1992) A kinetic study of immobilized lipase catalysing the synthesis of isoamyl acetate by transesterification in n-hexane. Enzyme Microbial Technology, 14, 709-714. doi:10.1016/0141-0229(92)90110-A

has been cited by the following article:

• TITLE: Optimization and kinetic modeling of lipase mediated enantioselective kinetic resolution of (±)-2-octanol

  AUTHORS: Jyoti B. Sontakke, Ganapati D. Yadav

  KEYWORDS: Immobilized Lipase; Novozyme 435; 2-Octanol; Response Surface Methodology; Kinetic Modeling; Enantioselectivity

  JOURNAL NAME: Natural Science, Vol.5 No.9, August 28, 2013

  ABSTRACT: Chiral 2-octanol is one of the key intermediates for preparation of liquid crystal materials, as well as many optically active pharmaceuticals. Lipase catalyzed kinetic resolution has proved to be an efficient technique for synthesis of enantiomerically enriched compounds. In the present study, optimization and kinetic modeling of kinetic resolution of (±)-2-octanol was done by using vinyl acetate as an acyl donor in n-heptane as a solvent. Response surface methodology (RSM) and four-factor-five-level Centre Composite Rotatable Design (CCRD) were employed to evaluate the effect of various parameters such as speed of agitation, enzyme loading, temperature and acyl donor/alcohol molar ratio on conversion, enantiomeric excess (ee), enantioselectivity and initial rate of reaction. Acylation of 2-octanol with vinyl acetate catalyzed by Novozyme 435 follows the ternary complex mechanism (ordered bi-bi mechanism) with inhibition by 2-octanol.