Cibacron Blue F3GA ligand dye-based magnetic silica particles for the albumin purification


Tatar N., AKGÖNÜLLÜ S., Yavuz H., DENİZLİ A.

Turkish Journal of Chemistry, cilt.47, sa.5, ss.1125-1137, 2023 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 47 Sayı: 5
  • Basım Tarihi: 2023
  • Doi Numarası: 10.55730/1300-0527.3599
  • Dergi Adı: Turkish Journal of Chemistry
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Chemical Abstracts Core, TR DİZİN (ULAKBİM)
  • Sayfa Sayıları: ss.1125-1137
  • Anahtar Kelimeler: Albumin purification, Cibacron blue F3GA, ligand dye, magnetic silica particles, protein purification
  • Hacettepe Üniversitesi Adresli: Evet

Özet

Dye-ligand affinity chromatography is among the increasingly popular affinity chromatography based on molecular recognition for the purification of albumin. This study focuses on the binding of Cibacron Blue F3GA ligand dye with magnetic silica particles and purification by separation. Mono-disperse silica particles with bimodal pore size distribution were employed as a high-performance adsorbent for human serum albumin (HSA) protein purification under equilibrium conditions. The synthesized ligand-dye affinity based magnetic silica particles were characterized by electron spin resonance, Fourier-transform infrared spectroscopy, scanning electron microscopy, vibrating sample magnetometer, elemental analysis, and dispersive X-ray analysis. The HSA purification performance of the proposed material in the presence of a magnetic field was relatively investigated using magnetic-based particles with similar morphologies. The maximum adsorption capacity for HSA in an artificial plasma medium was defined as 48.6 mg/g magnetic silica particle. By using the designed magnetic silica particles, 1.0 M NaCl solution was successfully utilized for obtaining quantitative desorption with HSA. However, continued HSA purification performances of magnetic-based particles were significantly lower concerning the ligand-dye magnetic silica particles. The purity of the removed albumin was about 97%. The magnetic silica particles could be utilized many times without decreasing their protein adsorption capacities remarkably.