Immobilization of lipase on mesoporous silica nanoparticles with hierarchical fibrous pore

Lipase from Candida Ragusa (CRL) was successfully covalently immobilized on fibrous silica nanoparticles KCC-1, and the properties of immobilized enzyme were investigated. Mesoporous fibrous silica nanoparticles (MSFIPs) were synthesized with particles size 200 nm pore size 15-30 nm: followed by amino-functionalization. Scanning Electron Microscopy (SEM), Transmittance Electronic microscopy (TEM), Fourier Transform Infrared Spectroscopy (FT-IR) and N-2 adsorption were used for the characterization of nanoparticles. Further SiO2@NH2 nanoparticles were activated by glutaraldehyde as a bifunctional cross linker, and were used for lipase immobilization. The applied approach for support preparation, activation, and optimization of immobilization conditions, led to better resistance to temperature and pH inactivation in comparison to the free lipase, and hence widened the reaction pH and temperature regions, with the optimum pH and temperature of 7.5 and 40 degrees C, respectively. The immobilized Lipase Candida Ragusa (ICRL) maintained above 81% of the initial activity after 28 days and 80% activity after 8 repeated cycles. Thus ICRL showed improved storage stability reusability and 700 U/g of protein as immobilization efficiency. (C) 2016 Elsevier B.V. All rights reserved.