Immobilization and Characterization of Hemoglobin on Modified Sporopollenin Surfaces
Yükleniyor...
Dosyalar
Tarih
2012
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Elsevier Science Bv
Erişim Hakkı
info:eu-repo/semantics/openAccess
Özet
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 degrees 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 degrees 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.
Açıklama
Anahtar Kelimeler
Sporopollenin, Hemoglobin, Modification, Silane, Horowitz-Metzger method
Kaynak
International Journal of Biological Macromolecules
WoS Q Değeri
Q3
Scopus Q Değeri
Q1
Cilt
50
Sayı
Künye
Gübbük, I. H., Özmen, M., Maltaş, E., (2012). Immobilization and Characterization of Hemoglobin on Modified Sporopollenin Surfaces. International Journal of Biological Macromolecules, (50), 1346-1352. Doi: 10.1016/j.ijbiomac.2012.04.009
