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Separation of Immunoglobulin G from Cheddar Cheese Whey by Avidin‐Biotinylated IgY Chromatography
Author(s) -
KIM H.,
LICHAN E. C. Y.
Publication year - 1998
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1998.tb15757.x
Subject(s) - biotinylation , avidin , chemistry , chromatography , elution , affinity chromatography , column chromatography , antibody , biotin , protein a , biochemistry , immunology , biology , enzyme
High‐purity immunoglobulins (Ig), which may be useful for immunologic supplementation of food products, were isolated from Cheddar cheese whey in a one‐step process using avidin‐biotinylated yolk immunoglobulin (IgY) column chromatography. Yolk antibodies specific to bovine IgG (IgY IgG ) were biotinylated with biotinyl amido‐hexanoic acid‐N‐hydroxy‐sulfo‐succinimide ester without any notable effect on antigen‐binding activity, and coupled to immobilized avidin columns. The resulting avidin‐biotinylated IgY IgG columns, with binding capacity of 50–55% (w/w percent ratio of IgG to immobilized IgY IgG ), were used for specific binding of IgG from cheese whey. Elution with a commercially available eluent (Actisep) or 0.1 M glycine‐HCl buffer at pH 2.8 yielded IgG with purity of 99% by radial immunodiffusion.