Micron-sized flower-like Fe₃O₄@GMA magnetic porous microspheres for lipase immobilization

Abstract

Flower-like Fe 3 O 4 microspheres prepared by a fast solvothermal method were selected to fabricate micron-sized Fe 3 O 4 @glycidyl methacrylate (GMA) magnetic porous microspheres. The magnetic porous microspheres were endowed with appropriate specific surface area (39.54 m 2 /g) and appropriate pore diameter (16 nm), which could be served as a carrier for immobilized lipase. Meanwhile, the prepared magnetic microspheres with high saturation magnetization could realize rapid separations. After those microspheres were aminated and activated, the obtained immobilized lipase possessed high efficiency of immobilization and catalytic activity, 2 with the optimum pH and temperature 8.0 and 40℃,respectively. The thermal stability of immobilized lipase was obviously exceed free lipase.

Fabrication of a magnetic nanoparticle embedded NH2-MIL-88B MOF hybrid for highly efficient covalent immobilization of lipase

“…The magnetic property was evaluated by using vibration sample magnetometry 9 (VSM) at 25 °C temperature by Lake Shore, Model-7410 magnetometer. The magnetic property was evaluated by using vibration sample magnetometry 9 (VSM) at 25 °C temperature by Lake Shore, Model-7410 magnetometer.…”

Preparation of light core/shell magnetic composite microspheres and their application for lipase immobilization

“…Recently, magnetic nanoparticles have aroused considerable research interest owing to the excellent magnetic responsiveness and their applications in different areas, such as separation and purification of proteins [1] , drug delivery [2] , cancer therapy [3] , imaging [4] , catalysis [5,6] , water treatment [7] , enzyme immobilization [8] , and so forth. Of all magnetic nanoparticles, magnetic Fe 3 O 4 microsphere is the most widely used due to its easy to separation and non-toxic.…”

Lipase Immobilized Metal‐Organic Frameworks as Remarkably Biocatalyst for Ester Hydrolysis: A One Step Approach for Lipase Immobilization

“…The immobilized CRL cannot transform the conformation easily during reaction condition which is possible for free CRL. So, after immobilization the active sites of CRL are more accessible for substrate than free lipase ,. The V max value of CRL is also decreased after in situ immobilization of lipase that means the rate of activity for immobilized enzyme slows down.…”