Protein adsorption and hydrodynamic stability of a dense, pellicular adsorbent in high-biomass expanded bed chromatography

Yen Mei Chow, Beng Ti Tey, Mohd Nordin Ibrahim, Arbakariya Ariff, Tau Chuan Ling

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5 Citations (Scopus)


A dense, pellicular UpFront adsorbent (p = 1.5 g/cm3, UpFront Chromatography, Copenhagen, Denmark) was characterized in terms of hydrodynamic properties and protein adsorption performance in expanded bed chromatography. Cibacron Blue 3GA was immobilised into the adsorbent and protein adsorption of bovine serum albumin (BSA) was selected to test the setup. The Bodenstein number and axial dispersion coefficient estimated for this dense pellicular adsorbent was 54 and 1.63 × 10-5 m2/s, respectively, indicating a stable expanded bed. It could be shown that the BSA protein was captured by the adsorbent in the presence of 30% (w/v) of whole-yeast cells with an estimated dynamic binding capacity (C/Co = 0.01) of approximately 6.5 mg/mL adsorbent.

Original languageEnglish
Pages (from-to)268-272
Number of pages5
JournalBiotechnology and Bioprocess Engineering
Issue number3
Publication statusPublished - May 2006
Externally publishedYes


  • Bovine serum albumin
  • Expanded bed chromatography
  • Hydrodynamic stability
  • Protein adsorption
  • Yeast cells

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