A surfactant-coated lipase immobilized in magnetic nanoparticles for multicycle ethyl isovalerate enzymatic production

• Published in: Biochemical engineering journal 2013-04, Vol.73, p.72-79
• Main Authors: Mahmood, Iram, Ahmad, Ishfaq, Chen, Guo, Huizhou, Liu
• Format: Article
• Language: English
• Subjects: anionic surfactants; biocatalysts; Biological and medical sciences; Biotechnology; Candida rugosa; coatings; coprecipitation; Esterification; flavor; Fourier transform infrared spectroscopy; Fundamental and applied biological sciences. Psychology; glutaraldehyde; Gum arabic; iron oxides; Lipase; Magnetic nanoparticles; nanoparticles; nonionic surfactants; particle size; solvents; temperature; transmission electron microscopy; X-ray diffraction
• ISSN: 1369-703X; 1873-295X
• DOI: 10.1016/j.bej.2013.01.017

► We design a new recyclable biocatalyst system for ethyl isovalerate production. ► System provides a combination of enzyme stability, recovery and reusability. ► 80% esterification yield in 48h was observed for non-ionic surfactant coated lipase. ► System retained higher catalytic activity (more than 65%) after reusing seven times. ► Enhanced activity due to interfacial activation was attained for this system. Gum arabic coated magnetic Fe3O4 nanoparticles (GAMNP) were prepared by chemical co-precipitation method and their surface morphology, particle size and presence of polymer-coating was confirmed by various measurements, including transmission electron microscopy (TEM), X-ray diffraction (XRD), thermo gravimetric analysis (TGA), and Fourier transform infra red (FTIR) analysis. Magnetic particles were employed for their potential application as a support material for lipase immobilization. Glutaraldehyde was used as a coupling agent for efficient binding of lipase onto the magnetic carrier. For this purpose, the surface of a Candida rugosa lipase was initially coated with various surfactants, to stabilize enzyme in its open form, and then immobilized on to the support. This immobilized system was used as a biocatalyst for ethyl isovalerate, a flavor ester, production. The influence of various factors such as type of surfactant, optimum temperature and pH requirement, organic solvent used, amount of surfactant in coating lipase and effect of enzyme loadings on the esterification reaction were systematically studied. Different surfactants were used amongst which non-ionic surfactant performed better, showing about 80% esterification yield in 48h as compared to cationic/anionic surfactants. Enhanced activity due to interfacial activation was observed for immobilized non-ionic surfactant–lipase complex. The immobilized surfactant coated lipase activity was retained after reusing seven times.