influence of a novel magnetic recoverable support on kinetic, stability and activity of beta-amylase enzyme

in this paper, covalent immobilization of beta amylase enzyme on the surface of modified magnetic nano particles (znfe2o4@sio2-nh2) is reported. for doing so, at first, the magnetic nanoparticles of znfe2o4 were synthesized by chemical co-precipitation method and then tetraethyl orthosilicate (teos) and 3-aminopropyltriethoxy silane (aptes) were used for modification of znfe2o4 nanoparticles with silica and amine groups (znfe2o4@sio2-nh2). then, the aminated surface of znfe2o4 nanoparticles was exposed to beta amylase immobilization using trichlorotriazine (tct) as covalent agent. the immobilized beta-amylase enzyme was characterized by techniques such as fourier transform infrared (ft-ir), scanning electron microscopy (sem), powder x-ray diffraction (xrd) and energy dispersive x-ray analysis (edax). the kinetics studies corroborate the michaelis-menten model and show much progress in the efficiency of immobilized enzyme compared to the free enzyme. also, the thermal stability of the beta-amylase enzyme is increased after immobilization. by applying a magnetic active support, simple and facile separation of beta-amylase from the reaction mixture and higher catalytic activity is possible. the highest activity for immobilized beta-amylase enzyme is observed at ph and temperature of 7.0 and 40 °c, respectively.