Investigation of steapsin lipase for kinetic resolution of secondary alcohols and synthesis of valuable acetates in non-aqueous reaction medium

In present study, the application of steapsin lipase (as a biocatalyst) was investigated for kinetic resolution of secondary alcohols (1-phenyl ethanol and their derivatives) using vinyl acetate as an activated acyl donor. The enzymatic protocol was optimized for various reaction parameters such as effect of the molar ratio, solvent, temperature, time and biocatalyst loading to obtain best reaction conditions. On optimization, developed enzymatic methodology provided considerable enantiomeric excess of the product (up to 92% ee) at 55 °C in n-hexane as a solvent. Furthermore using the developed protocol, synthesis of several industrially important acetates was successfully achieved with excellent yield (up to 99%). During acetate synthesis, the biocatalyst was remarkably reused for eight consecutive recycles without any significant loss in its catalytic activity. This revealed the good potential of steapsin lipase for application in organic solvents.

Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Steapsin lipase was investigated for kinetic resolution of sec-alcohols. ► Influence of various reaction parameters on kinetic resolution was studied. ► Synthesis of valuable flavour acetates was also successfully achieved. ► The biocatalyst was remarkably recycled for eight consecutive recycles. ► SEM analysis of steapsin lipase was performed for any distortion in appearance.