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原位改性法制备R Protein A亲和层析膜及对IgG分离纯化性能研究

杨栋 周丰 刘轲 李明月 张伊诺 李登科 程盼 朱绍存 朱丽萍 梅涛 向阳

纺织工程学报2026,Vol.4Issue(2):87-96,10.
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纺织工程学报2026,Vol.4Issue(2):87-96,10.DOI:10.20150/j.cnki.fzgcxb.2026.02.008

原位改性法制备R Protein A亲和层析膜及对IgG分离纯化性能研究

In-situ modification strategy for fabricating recombinant pro-tein a affinity chromatography membrane and its application in IgG separation

杨栋 1周丰 2刘轲 1李明月 1张伊诺 1李登科 1程盼 1朱绍存 3朱丽萍 4梅涛 5向阳2

作者信息

  • 1. 武汉纺织大学 纺织纤维及制品教育部重点实验室 纺织行业非织造过滤与分离材料重点实验室,湖北 武汉 430200
  • 2. 武汉纺织大学 纺织纤维及制品教育部重点实验室 纺织行业非织造过滤与分离材料重点实验室,湖北 武汉 430200||百威集团控股有限公司 安海斯布希企业管理(上海)有限公司武汉分公司,湖北 武汉 430051
  • 3. 山东泰鹏环保材料股份有限公司,山东 泰安 271699
  • 4. 东华大学 先进纤维材料全国重点实验室 材料科学与工程学院,上海 201620
  • 5. 武汉维晨科技有限公司,湖北 武汉 430106
  • 折叠

摘要

Abstract

Traditional Protein A affinity chromatography media employ resin bead materials with dense structures,high mass transfer resistance,and low flow rates.To address these limitations,constructed an affinity chromatography mem-brane composed of nanofibers.Ethylene-vinyl alcohol(EVOH)copolymer nanofibers were prepared via melt-blending phase separation,followed by slurry processing and vacuum filtration drying to fabricate the nanofiber membrane(NFM)support.Sodium hydroxide(NaOH)alkaline activation and sodium periodate(NaIO4)oxidation were applied to introduce aldehyde groups(CHO),enabling covalent immobilization of recombinant Protein A onto the membrane sur-face through in-situ reaction,yielding the affinity chromatography membrane(ONFM-3h-R).The effects of oxidant con-centration and reaction time on membrane morphology,chemical properties,hydrophilicity/hydrophobicity,and mechani-cal performance were investigated.Optimal preparation parameters and immunoglobulin G(IgG)separation perfor-mance were systematically evaluated.Results demonstrated that at 0.7 mol/L NaIO4 with 3 h oxidation,the resulting membrane(ONFM-3h)maintained well-preserved porous structures,achieved aldehyde group content of 0.85 mmol/g,exhibited favorable hydrophilicity,and demonstrated tensile stress of 3.62 MPa with 6.43%strain.Recombinant Protein A adsorption reached 8.90 mg/g.Furthermore,the affinity membrane showed an IgG adsorption capacity of 3.65 mg/g,specifically separated IgG from IgG-BSA mixed solutions,and maintained>90%adsorption capacity retention after three reuse cycles.This approach provides a novel strategy for enhancing the efficiency of traditional separation materi-als.

关键词

EVOH纳米纤维/重组蛋白A/原位反应/亲和层析膜/IgG分离纯化

Key words

EVOH nanofibers/recombinant Protein A/in-situ reaction/affinity chromatography membrane/IgG separa-tion and purification

分类

轻工纺织

引用本文复制引用

杨栋,周丰,刘轲,李明月,张伊诺,李登科,程盼,朱绍存,朱丽萍,梅涛,向阳..原位改性法制备R Protein A亲和层析膜及对IgG分离纯化性能研究[J].纺织工程学报,2026,4(2):87-96,10.

基金项目

国家自然科学基金项目(U23A20585,52273061) (U23A20585,52273061)

湖北省自然科学基金杰出青年项目(2023AFA086) (2023AFA086)

湖北省技术创新计划项目(2024BAB119) (2024BAB119)

武汉市科技计划项目(2023030103010633) (2023030103010633)

纺织工程学报

2095-4131

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