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Enzymatic fragmentation of cation exchange membrane bound immunoglobulin G
Author(s) -
Yu Deqiang,
Ghosh Raja
Publication year - 2010
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1002/btpr.501
Subject(s) - chemistry , membrane , fragmentation (computing) , chromatography , microporous material , enzyme , steric effects , macromolecule , reaction rate constant , stereochemistry , organic chemistry , kinetics , biochemistry , physics , quantum mechanics , computer science , operating system
Immunoglobulin G (IgG) was immobilized on a stack of microporous cation‐exchange membranes and pulsed with pepsin solution. Fc fragment and its sub‐fragments thus produced were removed along with the reaction flow‐through, whereas F(ab′) 2 which remained membrane bound could subsequently be eluted in a pure form using salt. The extent of IgG fragmentation and the apparent reaction rate constant were both significantly higher than in equivalent liquid phase reaction, presumably due to a combination of mass transport, steric, and substrate concentration effects. This approach of using a membrane surface as molecule cutting board could be attractive in niche applications such as integrated enzymatic reaction and purification processes involving macromolecular substrates. © 2010 American Institute of Chemical Engineers Biotechnol. Prog., 2011