Immobilization of Lipase on Mesoporous Silica Nanoparticles with Hierarchical Fibrous Pore

Publication date: Available online 13 October 2016 Source:Journal of Molecular Catalysis B: Enzymatic Author(s): Zafar Ali, Lei Tian, Panpan Zhao, Baoliang Zhang, Nisar Ali, Mohammad Khan, Qiuyu Zhang 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 (MSNPs) were synthesized with particles size 200nm pore size 15–30nm; followed by amino-functionalization. Scanning Electron Microscopy (SEM), transmittance electronic microscopy (TEM), Fourier Transform Infrared spectroscopy (FT-IR) and N2 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°C, respectively. The immobilized Lipase Candida Ragusa (ICRL) maintained above 81% of the initial activity after 28days and 80% activity after 8 repeated cycles. Thus ICRL showed improved storage stability reusability and 700U/g of protein as immobilization efficiency. Graphical abstract

Source: Journal of Molecular Catalysis B: Enzymatic - October 14, 2016 Category: Biochemistry Source Type: research