Expanded bed adsorption for Human Serum Albumin and Immunoglobulin G onto a cation exchanger mixed mode adsorbent

• Type: Article in International Scientific Journal
• Date: 2018

Authors

Pedro Ferreira Gomes (Author) FEUP; José Miguel Loureiro (Author) FEUP; Alírio E. Rodrigues (Author) FEUP

Journal

Title: Adsorption

Vol. 24 No. 3

Pages: 293-307

ISSN: 0929-5607

Publisher: Springer Nature

Indexing

ISI Web of Science

Scopus

INSPEC

Scientific classification

FOS: Engineering and technology > Chemical engineering

CORDIS: Technological sciences > Engineering > Chemical engineering

Other information

DOI: 10.1007/s10450-018-9940-7

Abstract (EN): Adsorption of human serum albumin (HSA) and immunoglobulin G (IgG), two most relevant proteins in blood serum were measured separately on a new mixed-mode adsorbent (MabDirect MM), especially designed for expanded bed adsorption process. Expanded bed behavior characterization by residence time distribution experiments for different columns (Streamline 50 for HSA study, Omnifit 66/20 and XK 16/20 for IgG study) are presented together with breakthrough adsorption of HSA and IgG for different conditions and compared with simulation results by a mathematical model. Regarding HSA adsorption, all four experiments were conducted at the same buffer solution (pH 5.0 without salt), and it was obtained a dynamic binding capacity of 8.9, 9.7, 7.5 and 7.0 mg center dot g(dry) (-1) (24.8, 27.0, 21.0 and 19.5 mg center dot cm(-3)) at 10% of breakthrough, corresponding to a 41, 39, 38 and 30% of the saturation capacity for runs 1-4, respectively. The results from the simulation of the mathematical model fitted well with the breakthrough experiments. Elution stage was optimized by lowering flow rate and changing the buffer solution pH and NaCl concentration. Concerning IgG adsorption, for IgG feed concentration of 0.53 g center dot dm(-3) in 20 mM citrate buffer, pH 5.0 with 0.4 M NaCl, at 2.2 cm(3)center dot min(-1), it was obtained a DBC of 3.3 mg center dot g(dry) (-1) (9.1 mg center dot cm(-3)) at 10% of breakthrough, representing 22% of the saturation capacity. While for a feed concentration of 0.11 g center dot dm(-3) of IgG in the same buffer solution, at 6 cm(3)center dot min(-1), it was obtained a DBC of 2.7 mg center dot g(dry) (-1) (7.4 mg center dot cm(-3)) at 10% of breakthrough, representing 34% of the saturation capacity.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 15