Immobilization and characterization of hemoglobin on modified sporopollenin surfaces

Hemoglobin was covalently immobilized onto modified sporopollenin surface with different functional groups by chemical reactions to enhance binding ability of protein. In this study, the influence of various silane linker molecules on the capacity of protein binding was studied. For this purpose, activated sporopollenin was modified by 3-aminopropyltriethoxysilane (APTS), 3-chloropropyltrimethoxysilane (CPTS) and (3-glycidyloxypropyl)trimethoxysilane (GPTS). Hemoglobin (Hb) was immobilized on modified sporopollenin surfaces in phosphate buffer saline solution (PBS, pH 7.4) at 4 °C. Results showed that GPTS modified sporopollenin surfaces resulted in the highest binding capacity for Hb. Micro porosity of samples was observed through scanning electron microscopy (SEM) and thermal behavior of the samples were studied with thermogravimetric analysis (TGA) within a temperature range: 25–900 °C. TGA studies demonstrated the advantages of silane modification for high temperature applications and illustrated differences of the structures due to the different tail groups.