Improving efficiency and reducing enzyme inactivation during lipase-mediated epoxidation of α-pinene in a double-phase reaction system

Chemoenzymatic epoxidation of olefin mediated by lipase is a green and environmentally friendly alternative process. However, the mass transfer barrier and lipase deactivation caused by the traditional organic-water biphasic reaction system have always been the focus of researchers' attention. To overcome these issues, we investigated the effects of reaction temperature and two important substrates (H2O2 and acyl donor) on the epoxidation reaction and interfacial mass transfer. As a result, we determined the optimal reaction conditions: a temperature of 30 ?, 30 wt-% H2O2 as the oxygen source, and 1 M lauric acid as the oxygen carrier. Additionally, by simulating the conditions of shaking flask reactions, we designed a batch reactor and added a metal mesh to effectively block the direct contact between high-concentration hydrogen peroxide and the enzyme. Under these optimal conditions, the epoxidation reaction was carried out for 5 h, and the product yield reached a maximum of 93.2%. Furthermore, after seven repetitive experiments, the lipase still maintained a relative activity of 51.2%.

Automated summary

The chemoenzymatic epoxidation of olefin mediated by lipase is an environmentally friendly alternative process. In this study, we investigated the effects of reaction temperature and two substrates on the epoxidation reaction and interfacial mass transfer. Optimal conditions were determined and a batch reactor with a metal mesh was designed to block direct contact between high-concentration hydrogen peroxide and the enzyme. Under these conditions, a maximum product yield of 93.2% was achieved and the lipase maintained a relative activity of 51.2% after repetitive experiments.