关键词: Epoxidation Lipase Reactor α-Pinene

Mesh : Lipase Hydrogen Peroxide Bicyclic Monoterpenes Alkenes

来  源:   DOI:10.1007/s00449-023-02902-4

Abstract:
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 °C, 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%.
摘要:
脂肪酶介导的烯烃化学酶环氧化是一种绿色环保的替代工艺。然而,传统的有机-水两相反应体系引起的传质屏障和脂肪酶失活一直是研究者关注的焦点。为了克服这些问题,我们研究了反应温度和两种重要底物(H2O2和酰基供体)对环氧化反应和界面传质的影响。因此,我们确定了最佳反应条件:温度为30°C,30重量%H2O2作为氧源,和1M月桂酸作为氧载体。此外,通过模拟摇瓶反应的条件,我们设计了间歇式反应器,并添加了金属网,以有效地阻止高浓度过氧化氢与酶之间的直接接触。在这些最佳条件下,环氧化反应进行5h,产品收率最高达93.2%。此外,经过七个重复的实验,脂肪酶仍保持51.2%的相对活性。
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