%0 Journal Article
%T Enzymatic Production of Biodiesel Using Immobilized Lipase on Core-Shell Structured Fe3O4@MIL-100(Fe) Composites
%J Catalysts | An Open Access Journal from MDPI
%D 2019
%R https://doi.org/10.3390/catal9100850
%X In this research, core¨Cshell structured Fe 3O 4@MIL-100(Fe) composites were prepared by coating Fe 3O 4 magnetite with porous MIL-100(Fe) metal-organic framework (MOF) material, which were then utilized as magnetic supports for the covalent immobilization of the lipase from Candida rugosa through amide linkages. By using the carbodiimide/hydroxysulfosuccinimide (EDC/NHS) activation strategy, the lipase immobilization efficiency could reach 83.1%, with an activity recovery of 63.5%. The magnetic Fe 3O 4@MIL-100(Fe) composite and immobilized lipase were characterized by several techniques. The characterization results showed that the Fe 3O 4 core was coated with MIL-100(Fe) shell with the formation of perfect core¨Cshell structured composites, and moreover, the lipase was covalently tethered on the magnetic carrier. The immobilized lipase displayed a strong magnetic response and could be facilely separated by an external magnetic field. With this magnetic biocatalyst, the maximum biodiesel conversion attained 92.3% at a methanol/oil molar ratio of 4:1, with a three-step methanol addition manner, and a reaction temperature of 40 ˇăC. Moreover, the biocatalyst prepared in the present study was recycled easily by magnetic separation without significant mass loss, and displayed 83.6% of its initial activity as it was reused for five runs, thus allowing its potential application for the cleaner production of biodiesel. View Full-Tex
%U https://www.mdpi.com/2073-4344/9/10/850