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Isolation of immunoglobulin G from bovine milk whey by poly(hydroxyethyl methacrylate)‐based anion‐exchange cryogel
Author(s) -
Dong Shasha,
Chen Liang,
Dai Bin,
Johnson Wilfred,
Ye Jialei,
Shen Shaochuan,
Yun Junxian,
Yao Kejian,
Lin DongQiang,
Yao ShanJing
Publication year - 2013
Publication title -
journal of separation science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.72
H-Index - 102
eISSN - 1615-9314
pISSN - 1615-9306
DOI - 10.1002/jssc.201300306
Subject(s) - chemistry , bovine milk , isolation (microbiology) , methacrylate , (hydroxyethyl)methacrylate , ion exchange , 2 hydroxyethyl methacrylate , whey protein , chromatography , antibody , ion exchange resin , microbiology and biotechnology , polymer , ion , organic chemistry , monomer , biology , immunology
Bovine milk whey contains several bioactive proteins such as α‐lactalbumin, β‐lactoglobulin, and immunoglobulin G ( I g G) . Chromatographic separation of these proteins has received much attention in the past few years. In this work, we provide a chromatographic method for the efficient isolation of I g G from bovine milk whey using a poly(2‐hydroxyethyl methacrylate)‐based anion‐exchange cryogel. The monolithic cryogel was prepared by grafting 2‐(dimethylamino) ethyl methacrylate onto the poly(2‐hydroxyethyl methacrylate)‐based cryogel matrix and then employed to separate I g G under various buffer pH and salt elution conditions. The results showed that the buffer pH and the salt concentration in the step elution have remarkable influences on the purity of I g G , while the I g G recovery depended mainly on the loading volume of whey for a given cryogel bed. High purity I g G (more than 95%) was obtained using the phosphate buffer with pH of 5.8 as the running buffer and the salt solution in as the elution liquid. With suitable loading volume of whey, the maximum I g G recovery of about 94% was observed. The present separation method is thus a potential choice for the isolation of high‐purity I g G from bovine milk whey.