Salt-enhanced permeabilization for monoclonal antibody precipitation and purification in a tubular reactor with a depth filtration membrane with advanced chromatin extraction

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12520%2F19%3A43900793" target="_blank" >RIV/60076658:12520/19:43900793 - isvavai.cz</a>

Result on the web

<a href="https://www.sciencedirect.com/science/article/pii/S1369703X19302670" target="_blank" >https://www.sciencedirect.com/science/article/pii/S1369703X19302670</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bej.2019.107332" target="_blank" >10.1016/j.bej.2019.107332</a>

Result language

angličtina

Original language name

Salt-enhanced permeabilization for monoclonal antibody precipitation and purification in a tubular reactor with a depth filtration membrane with advanced chromatin extraction

Original language description

Non-protein A-based purification technology is increasingly needed in that protein A chromatography possesses mang inherent problems, such as the high material and operational costs, limited productivity, and leaching of the protein A ligand. In this study, antibody purification was first achieved by precipitation of the antibody from the cell culture supernatant (CCS) in a tubular reactor with a static mixer. The protein precipitates were efficiently intercepted by incorporating a depth filtration membrane directly after the mixer. Chromatin-directed cell culture clarification was shown to enable the full usage of the load of the filter membrane and also significantly reduced the burden of the subsequent purification step. The addition of NaCl to the CCS significantly increased the permeabilization of the filter membrane by increasing the loading capacity by up to 20%. The redissolved and eluted antibodies were further polished using single multimodal chromatography, which supported direct sample loading. The content of non-histone host cell protein (n-h-HCP) in the final product was less than 20 ppm, DNA was less than 1 ppb, and the aggregates was less than 0.05%. The overall antibody recovery was (similar to)82%. This method is a feasible alternative to the current protein A-dominant antibody purification platform and has high value and potential for widespread implementation.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10617 - Marine biology, freshwater biology, limnology

Project

—

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2019

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Biochemical engineering journal

ISSN

1873-295X

e-ISSN

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Volume of the periodical

151

Issue of the periodical within the volume

neuveden

Country of publishing house

NL - THE KINGDOM OF THE NETHERLANDS

Number of pages

11

Pages from-to

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UT code for WoS article

000518140400037

EID of the result in the Scopus database

2-s2.0-85070583987