In-situ stabilized lipase in calcium carbonate microparticles for activation in solvent-free transesterification for biodiesel production

被引:4
作者
Choi, Young Sik [1 ]
Jeon, Hyo Won [1 ]
Hwang, Ee Taek [1 ]
机构
[1] Dong A Univ, Dept Food Biotechnol, Busan 49315, South Korea
基金
新加坡国家研究基金会;
关键词
Biodiesel; Solvent-free transesterification; Lipase immobilization; Calcium carbonate; Lipase activation; INTERFACIAL ACTIVATION; IMMOBILIZATION; ENZYME; FUEL;
D O I
10.1016/j.biortech.2024.131394
中图分类号
S2 [农业工程];
学科分类号
0828 ;
摘要
Biodiesel serves as a crucial biofuel alternative to petroleum-based diesel fuels, achieved through enzymatic transesterification of oil substrates. This study aims to investigate stabilized lipase (LP) within calcium carbonate (CaCO3) microparticles as a catalyst for solvent-free transesterification in biodiesel synthesis. The specific hydrolysis activity of the in-situ immobilized LP was 66% of that of free LP. However, the specific transesterification activity of immobilized LP in the solvent-free phase for biodiesel production was 2.29 times higher than that of free LP. These results suggest that the interfacial activation of LP molecules is facilitated by the inorganic CaCO3 environment. The immobilized LP demonstrated higher biodiesel production levels with superior stability compared to free LP, particularly regarding methanol molar ratio and temperature. To the best of our knowledge, there are no previous reports on the in-situ immobilization of LP in a CaCO3 carrier without any crosslinker as an interfacial-activated biocatalyst for biodiesel production.
引用
收藏
页数:10
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