Polyethylene glycol diacrylate-based supermacroporous monolithic cryogel as high-performance liquid chromatography stationary phase for protein and polymeric nanoparticle separation

被引:36
|
作者
Chen, Zhiyong [1 ]
Xu, Li [2 ]
Liang, Yuan [1 ]
Wang, Jianbin [1 ]
Zhao, Meiping [1 ]
Li, Yuanzong [1 ]
机构
[1] Peking Univ, Coll Chem & Mol Engn, Key Lab Bioorgan Chem & Mol Engn, BNLMS, Beijing 100871, Peoples R China
[2] Peking Univ, Coll Life Sci, Natl Lab Prot Engn & Plant Genet engn, Beijing 100871, Peoples R China
基金
中国国家自然科学基金;
关键词
HPLC; monolith; cryogel; nanoparticle; protein; AFFINITY; PURIFICATION; COLUMNS;
D O I
10.1016/j.chroma.2007.12.084
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
A supermacroporous monolithic cryogel was directly prepared by in situ cryo-copolymerization in a stainless steel cartridge (70 mm x 5.0 mm I.D.) using methacrylic acid (MAA) as functional monomer;and polyethylene glycol diacrylate (PEGDA) as crosslinker. The highly crosslinked (90%, molar ratio) poly(MAA-PEGDA) cryogel had more uniform supermacropores with a mean diameter of 25 p,m compared to the poly(acrylamide)-based cryogels. The viability of poly(MAA-PEGDA) cryogel as a medium was demonstrated for separations of lysozyme from chicken egg white (CEW) and water-soluble poly(N-isopropylacrylamide-co-3-(dimethylamino) propyl methacrylamide) (NIPAM-DMAPMA) nanoparticles from its crude reaction solution. The dynamic binding capacities of lysozyme and the polymeric nanoparticles were 4.51 x 10(-3) mu mol/ml and 33.4 mu g/ml, respectively. The lysozyme recovered from the above separations had a purity of more than 85%, and retained 90% of its enzymatic activity. (c) 2008 Elsevier B.V. All rights reserved.
引用
收藏
页码:128 / 131
页数:4
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