Syntheses, characterization of polymeric-Schiff base including aminoacid and it?s Ni(II) complexes and immobilization

In this study, polymer-bound Schiff bases (FMPS-Ala-Sch) and it?s Ni(II) complex were synthesized from alanine and (4-formyl-3-methoxyphenoxymethyl)polystyrene (FMPS). The structure of polymer-bound Schiff bases were characterized elemental analysis, thermogravimetry (TGA), scanning electron microscopy (SEM) and spectrum of UV-GB. ß-Galactosidase was immobilized onto the (FMPS), (FMPS-Ala-Sch) and (FMPS-Ala-Sch-Ni) complexes with using the covalent binding. The influence of temperature, pH, and storage capacity on the free and immobilized ß-galactosidase was investigated. In addition, reusability of immobilized ß-galactosidase was studied. The Km / Vmax values were calculated as 0.343mM/ 0.0259 mMmin?1 for free ß-galactosidase and 0.104 mM / 0.0126 mMmin?1, 0.0617 mM / 0.0417 mMmin?1 and 0.210 mM / 0.0287 mMmin?1 for ß-galactosidase immobilized to the (FMPS), (FMPS-Ala-Sch) and (FMPS-Ala-Sch-Ni) supports respectively. The storage capacity of (FMPS-Ala-Sch-Ni) was found higher than that of the other polymers.