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One-step purification of alpha(1)-antitrypsin by regulating polyelectrolyte ligands on mussel-inspired membrane adsorber
Fan, Jinxin1,2; Luo, Jianquan1,2; Song, Weijie1; Wan, Yinhua1,2
2017-04-15
Source PublicationJOURNAL OF MEMBRANE SCIENCE
ISSN0376-7388
Volume528Pages:155-162
Abstract

One-step purification of biomolecules from complex feed is challenging with commercial membrane adsorbers since it is difficult to screen and regulate the ligands on the membrane with traditional techniques for removal of various impurities. By readily grafting cationic polyelectrolyte ligands on a polydopamine (PDA)-coated membrane, a membrane adsorber with suitable ligand (750 kDa polyethylenimine, PEI) was selected to achieve one-step purification of arantitrypsin (AAT) from pretreated human plasma fraction W. It was found that ligand structure and molecular weight showed a significant effect on the properties and separation performance of membrane adsorbers. The attached polyelectrolytes increased membrane hydrophilicity but caused an enhancement of filtration resistance, and quaternization of the ligands (PEI and polyallylamine) further improved the hydrophilicity but decreased the charge quantity. By further screening elution salt concentration, flow rate, buffer pH, loading volume as well as molecular weight of PEI ligands, a high activity recovery of 96.6% and a high purity of 94.6% of AAT were obtained by one-step membrane chromatography, which was even better than those by multiple-step method. This could be owing to the special multilayer structure of PEI chains, which could suppress the impurity protein binding on the adsorption sites by exclusion effect. The present work not only provides new insights into the purification of biomolecules from complex streams with polyelectrolytecoupled membrane adsorbers, but also offers a new approach to design the ligands on membrane adsorber for specific application.

KeywordAlpha(1)-arantitrypsin Cationic Polyelectrolyte Polydopamine Anion-exchange Membrane Adsorber Membrane Chromatography
SubtypeArticle
WOS HeadingsScience & Technology ; Technology ; Physical Sciences
DOI10.1016/j.memsci.2017.01.037
Indexed BySCI
Language英语
WOS KeywordMixed Matrix Membrane ; Transfer Radical Polymerization ; Ion-exchange Chromatography ; Hollow-fiber Membrane ; Protein-binding ; Human-plasma ; Inhibitor Concentrate ; Fouling-resistant ; High-capacity ; Separation
WOS Research AreaEngineering ; Polymer Science
WOS SubjectEngineering, Chemical ; Polymer Science
Funding OrganizationNational High Technology Research and Development Program of China (863 Program)(2014AA021006 ; Youth Innovation Promotion Association of Chinese Academy of Sciences(2017069) ; 2014AA022206)
WOS IDWOS:000395956400016
Citation statistics
Document Type期刊论文
Identifierhttp://ir.ipe.ac.cn/handle/122111/22138
Collection生化工程国家重点实验室
Affiliation1.Chinese Acad Sci, Inst Proc Engn, State Key Lab Biochem Engn, Beijing 100190, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
Recommended Citation
GB/T 7714
Fan, Jinxin,Luo, Jianquan,Song, Weijie,et al. One-step purification of alpha(1)-antitrypsin by regulating polyelectrolyte ligands on mussel-inspired membrane adsorber[J]. JOURNAL OF MEMBRANE SCIENCE,2017,528:155-162.
APA Fan, Jinxin,Luo, Jianquan,Song, Weijie,&Wan, Yinhua.(2017).One-step purification of alpha(1)-antitrypsin by regulating polyelectrolyte ligands on mussel-inspired membrane adsorber.JOURNAL OF MEMBRANE SCIENCE,528,155-162.
MLA Fan, Jinxin,et al."One-step purification of alpha(1)-antitrypsin by regulating polyelectrolyte ligands on mussel-inspired membrane adsorber".JOURNAL OF MEMBRANE SCIENCE 528(2017):155-162.
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