Evaluation of mixed-mode chromatographic resins for separating IgG from serum albumin containing feedstock

Wang, Rong-Zhu; Lin, Dong‐Qiang; Tong, Hong-Fei; Lu, Haijun; Yao, Shan-Jing

doi:10.1016/j.jchromb.2013.07.029

Cited by 29 publications

(19 citation statements)

References 41 publications

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“…The SEC-HPLC results showed that the purity of hIgG was 99.7% and the recovery was 94.6%. Our previous work using commercial resins MEP HyperCel [15,29] and Bestarose Diamond MMA [29] showed bIgG purities of 90.0-97.0% with recovery of 82.4-87.7% under similar experimental conditions. Therefore, KB-ABI studied showed better performance on both IgG purity and recovery.…”

Section: Purification Of Higg From Protein Mixturesmentioning

confidence: 66%

Hydrophobic charge‐induction resin with 5‐aminobenzimidazol as the functional ligand: preparation, protein adsorption and immunoglobulin G purification

Yan

Zhang

Tong

et al. 2015

J of Separation Science

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A new hydrophobic charge-induction chromatography resin was prepared with 5-aminobenzimidazol as functional ligand and polyacrylic ester beads as matrix. Adsorption isotherms and adsorption in columns were investigated using human immunoglobulin G and bovine serum albumin as model proteins, and the influence of pH and NaCl concentration was discussed. Results showed that the ligand density was 195 μmol/mL gel, and protein selectivity can be improved by controlling pH and salt addition. An optimized purification process (sample loading at pH 8.0 with 0.2 M NaCl and elution at pH 5.0) was performed to purify human immunoglobulin G from bovine serum albumin containing feedstock, which resulted in human immunoglobulin G purity of 99.7% and recovery of 94.6%. A similar process was applied for the purification of monoclonal antibody from cell culture supernatant, which showed antibody purity of 94.9% and recovery of 92.5%. The results indicated that the new resin developed had comparable performance as Protein A chromatography and would be suitable for antibody purification from complex feedstock.

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Section: Purification Of Higg From Protein Mixturesmentioning

confidence: 66%

Hydrophobic charge‐induction resin with 5‐aminobenzimidazol as the functional ligand: preparation, protein adsorption and immunoglobulin G purification

Yan

Zhang

Tong

et al. 2015

J of Separation Science

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“…A separate study evaluated four different commercially available mixed-mode ligands -N-benzyl-N-methyl ethanol amine (Bestarose Diamond MMA), 2-benzamiodo-4-mercaptobutanoic acid (Bestarose Diamond MMC), 4-mercapto ethylpyridine (MEP HyperCel), and phenylpropylamine (PPA HyperCel) -for their ability to separate IgG from serum albumin under pH gradient elution. 4 The study showed that Bestarose Diamond MMA (Diamond MMA, Northbrook, IL, USA) outperformed the other ligands, achieving an IgG purity of 99.0% and recovering 89.5%. 4 The use of mixedmode ligands facilitated the control of elution by controlling pH.…”

Section: Multimodal (Mixed-mode) Affinity Chromatographymentioning

confidence: 99%

“…4 The study showed that Bestarose Diamond MMA (Diamond MMA, Northbrook, IL, USA) outperformed the other ligands, achieving an IgG purity of 99.0% and recovering 89.5%. 4 The use of mixedmode ligands facilitated the control of elution by controlling pH. Tong et al 60 found that the addition of caprylate as an albumin-selective moiety improved IgG yield during HCIC.…”

Section: Multimodal (Mixed-mode) Affinity Chromatographymentioning

confidence: 99%

“…However, at present, there is a movement away from the use of bioaffinity ligands such as Protein A, because of a number of limiting factors such as the leakage of Protein A from the column with associated product contamination, high cost, low reusability of resin, and putative antibody aggregation during low pH elution. [2][3][4] Purification can alternatively be achieved through the use of genetically fused purification tags, the most common of which is a polyhistidine tag (poly-His or His 6 ) that is utilized in immobilized metal affinity chromatography (IMAC). The production of a poly-His tag exerts a low metabolic burden on the producing host; however, it is not as specific as affinity chromatography.…”

Section: Introductionmentioning

confidence: 99%

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Technology advancements in antibody purification

Murphy¹,

Devine²,

O’Kennedy³

2016

ANTI

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Abstract:The separation of antibodies from complex mixtures can be achieved using chromatographic or non-chromatographic techniques. The purification of antibodies using chromatography involves the separation of antibodies or antibody-derived molecules present in complex mixtures by passing them through a solid phase (eg, silica resin or beads, monolithic columns, or cellulose membranes) and allowing the antibodies to bind or pass through depending on whether "bind-and-elute" or "flow-through" chromatographic methods are employed. Chromatographic methodologies can incorporate different separation techniques, such as affinity-tag binding, ion-exchange, size-exclusion chromatography, or immunoaffinity chromatography. However, in a concerted effort to become less reliant on chromatography-based separations owing to the high cost of large-scale production, non-chromatographic-based techniques such as precipitation, flocculation, crystallization, filtration, and aqueous two-phase partitioning are now becoming more popular. This review details current chromatographic and non-chromatographic methodo logies used for the purification of antibodies and expands on technological advancements and practical uses that have recently been reported.

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“…The latter also extended further for modeling the protein retentions in mixed-mode chromatography for isocratic and gradient elution in a wide range of pH and salt concentration [38]. Elution method based on pH gradient or pH step changes has also been proposed to increase the elution efficiency and selectivity [39][40]. While both the understanding of protein interaction with ligand and the control of pH gradient elution requires a precise description of the ligand response to pH, works regarding the determination of resin pKa and ionization model is lacked.…”

Section: Multimodal Chromatographymentioning

confidence: 99%

Protein Adsorption and Transport in Novel Chromatographic Anion Exchange and Multimodal Resins

Zhu¹

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Understanding the mechanism of protein adsorption and transport and the effects of the stationary phase architecture are critical for the optimum design of chromatographic processes.This work studies the properties of novel stationary phases that are based on a rigid macroporous backbone matrix synthesized with hydrophilic polymers (UNOsphere), which can be functionalized with a variety of ligands. Cationic ligands introduced with a range of grafted polymeric surface extenders as well as multimodal anionic ligands are considered. Both macroscopic and microscopic studies of particle properties, as well as orthogonal measurements of protein adsorption isotherms and kinetics, are used to understand these materials.Characterizations of anion exchangers with no polymer grafts (UNO Q), moderate graft content (Nuvia HR Q), and high graft content (Nuvia Q) show the pore volume accessible by

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Evaluation of mixed-mode chromatographic resins for separating IgG from serum albumin containing feedstock

Cited by 29 publications

References 41 publications

Hydrophobic charge‐induction resin with 5‐aminobenzimidazol as the functional ligand: preparation, protein adsorption and immunoglobulin G purification

Hydrophobic charge‐induction resin with 5‐aminobenzimidazol as the functional ligand: preparation, protein adsorption and immunoglobulin G purification

Technology advancements in antibody purification

Protein Adsorption and Transport in Novel Chromatographic Anion Exchange and Multimodal Resins

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