Rhizopus oryzae lipase(ROL)was immobilized on the surface of silica coated amino modified CoFe_(2)O_4 nanoparticles and applied for biodiesel production.The results indicated more affinity of the ROL toward its substr...Rhizopus oryzae lipase(ROL)was immobilized on the surface of silica coated amino modified CoFe_(2)O_4 nanoparticles and applied for biodiesel production.The results indicated more affinity of the ROL toward its substrate upon immobilization,as revealed by a lower Km value for the immobilized ROL compared to its free counterpart.Intrinsic fluorescence spectroscopy indicated a lower intensity for ROL immobilized on CoFe_(2)O_4 nanoparticles.Besides,immobilized ROL steady state anisotropy measurements presented lower values,which implied assembly of ROL molecules on magnetic nanoparticles upon immobilization as well as their restricted rotation upon covalent attachment.Thermal stability analysis revealed improved activity at higher temperatures for the immobilized enzyme compared to its free counterpart.Accordingly,Pace analysis to determine protein thermal stability revealed preservation of the protein conformation in the presence of increasing temperatures upon immobilization on nanoparticles.Finally,ROL immobilized on CoFe_(2)O_(4)nanoparticles exhibited improved efficiency of biodiesel production in agreement with thermal activity profile.Therefore,the authors suggest application of the lipase molecules immobilized on CoFe_(2)O_(4)nanoparticles for more efficient biodiesel production.展开更多
基金financially supported by Research Institute of Applied Science(RIAS)ACECRInstitute of Biochemistry and Biophysics(IBB)Iran National Science Foundation(INSF)。
文摘Rhizopus oryzae lipase(ROL)was immobilized on the surface of silica coated amino modified CoFe_(2)O_4 nanoparticles and applied for biodiesel production.The results indicated more affinity of the ROL toward its substrate upon immobilization,as revealed by a lower Km value for the immobilized ROL compared to its free counterpart.Intrinsic fluorescence spectroscopy indicated a lower intensity for ROL immobilized on CoFe_(2)O_4 nanoparticles.Besides,immobilized ROL steady state anisotropy measurements presented lower values,which implied assembly of ROL molecules on magnetic nanoparticles upon immobilization as well as their restricted rotation upon covalent attachment.Thermal stability analysis revealed improved activity at higher temperatures for the immobilized enzyme compared to its free counterpart.Accordingly,Pace analysis to determine protein thermal stability revealed preservation of the protein conformation in the presence of increasing temperatures upon immobilization on nanoparticles.Finally,ROL immobilized on CoFe_(2)O_(4)nanoparticles exhibited improved efficiency of biodiesel production in agreement with thermal activity profile.Therefore,the authors suggest application of the lipase molecules immobilized on CoFe_(2)O_(4)nanoparticles for more efficient biodiesel production.
