Hydrophobic interaction chromatography as polishing step enables obtaining ultra-pure recombinant antibodies

Autor(es)

Antunes Pereira Bresolin, Iara Rocha ^{[1, 2]} ; Lingg, Nico ^{[2, 3]} ; Lazzarotto Bresolin, Igor Tadeu ^{[1, 2]} ; Jungbauer, Alois ^{[2, 3]}

Afiliação do(s) autor(es)

^[1] Univ Fed Sao Paulo, Chem Engn Dept, Diadema, SP - Brazil

^[2] Univ Nat Resources & Life Sci, Inst Bioproc Sci & Engn, Vienna - Austria

^[3] Austrian Ctr Ind Biotechnol ACIB, Vienna - Austria

• Tipo de documento: Artigo Científico
• Fonte: Journal of Biotechnology; v. 324, n. S 2020.
• Citações Web of Science: 1

Resumo

Hydrophobic interaction chromatography is a versatile method to polish antibodies. Here, we present a polishing procedure in order to obtain an ultra-pure preparation of antitumor necrosis factor (TNF) alpha IgG1. Hydrophobic interaction chromatography (HIC) was used with Toyopearl (R) Phenyl 650 Madsorbent in the presence of ammonium sulfate. Adsorption isotherms, breakthrough curves and chromatographic runs were carried out. The eluted antibody was recovered with 99.9% purity and 96.2% yield. In the main peak, aggregates, host cell proteins (HCP) and DNA content were below the limit of detection of the analytical methods used. Thus, the method proposed here shows potential to be employed in a downstream process when an ultra-pure antibody preparation is required. (AU)

• Processo FAPESP: 18/16533-1 - Recuperação e purificação de anticorpos monoclonais por processos de cromatografia contínua de interação hidrofóbica
• Beneficiário: Iara Rocha Antunes Pereira Bresolin
• Modalidade de apoio: Bolsas no Exterior - Pesquisa