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

被引:3
作者
Yu, Lishuang [1 ]
Zou, Cheng [1 ]
Li, Qingyun [1 ,2 ]
Liu, Zhaoming [3 ]
Liu, Youyan [1 ,2 ]
Tang, Aixing [1 ,2 ]
机构
[1] Guangxi Univ, Sch Chem & Chem Engn, Nanning 530004, Peoples R China
[2] Guangxi Univ, Key Lab Guangxi Biorefinery, Nanning 530004, Peoples R China
[3] Guangxi Agr Vocat Univ, Sch Econ & Management, Nanning 530007, Peoples R China
基金
中国国家自然科学基金;
关键词
& alpha; -Pinene; Epoxidation; Lipase; Reactor; HYDROGEN-PEROXIDE; ALPHA-PINENE; CHEMOENZYMATIC EPOXIDATION; MONOTERPENES; ALKENES; ACID;
D O I
10.1007/s00449-023-02902-4
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
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%.
引用
收藏
页码:1331 / 1340
页数:10
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