Biocatalytic Epoxidation of Cyclooctene to 1,2-Epoxycyclooctane by a Newly Immobilized Aspergillus niger Lipase

Abstract

A newly immobilized Aspergillus niger lipase (ANL@ZnGlu-MNPs) was employed for the preparation of 1,2-epoxycyclooctane by oxidation of cyclooctene. The chosen variables, including substrate concentration, reaction temperature, immobilized enzyme dose, and H2O2 dose, were optimized in the reaction system of ethyl acetate. The yield and the enantiomeric excess of the product were achieved at 56.8% and 84.1%, respectively, under the following optimum reaction conditions: the concentration of substrate (cyclooctene) was 150 mM, the dosages of immobilized enzyme (ANL@ZnGlu-MNPs) and hydrogen peroxide were respectively 100 mg and 4.4 mmol, and the reaction was carried out in the system of 4 mL ethyl acetate at 40 °C. Further study on the operational stability of ANL@ZnGlu-MNPs showed that more than 51.6% of product yield was obtained after reusing for ten batches. A novel immobilized lipase was prepared and applied to synthesize 1,2-epoxycyclooctane from cyclooctene. Although ANL@ZnGlu-MNPs performs well in operational stability and the reaction can achieve high enantiomeric purity of the product, the yield of the catalytic reaction needs to be further improved.