Characterization of Superparamagnetic Iron Oxide Nanoparticles and Its Application in Protein Purification
2011 (English)In: Journal of Nanoscience and Nanotechnology, ISSN 1533-4880, Vol. 11, no 11, 10201-10206 p.Article in journal (Refereed) Published
The application of surface modified magnetic adsorbent particles in combination with magnetic separation techniques has received considerable awareness in recent years. There is a particular need in protein purification and analysis for specific, functional and generic methods of protein binding on solid supports. Nanoscale superparamagnetic iron oxide particles have been used to purify a natural coagulant protein extracted from Moringa oleiferaseeds. Spectrophotometric analysis of the coagulant protein was performed using synthetic clay solution as substrate. Protein binding with carboxyl and silica surface modified superparamagnetic iron oxide nanoparticles (SPION) were compared with the known carboxyl methyl cellulose (CMC) beads of ∼1 m. SPION modified with carboxyl surface showed higher binding capacity towards the coagulant protein compared to the CMC beads. The high surface area to volume ratio of the carboxyl-coated SPION resulted in high binding capacity and rapid adsorption kinetics of the crude protein extract. The purification and molecular weight of coagulant protein is analyzed by SDS-PAGE. This approach utilizes the most efficient, feasible and economical method of coagulant protein purification and it can also be applicable to other proteins that possess similar properties.
Place, publisher, year, edition, pages
American Scientific Publishers, 2011. Vol. 11, no 11, 10201-10206 p.
Coagulation Activity, Nanoscale, Immobilization, Surface Effect, Magnetic Adsorbent
IdentifiersURN: urn:nbn:se:kth:diva-59580DOI: 10.1166/jnn.2011.5007ISI: 000298765800152ScopusID: 2-s2.0-84857174054OAI: oai:DiVA.org:kth-59580DiVA: diva2:475966
QC 201201192012-01-192012-01-112012-05-09Bibliographically approved