中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Recovery of human serum albumin by dual-mode chromatography from the waste stream of Cohn fraction V supernatant

文献类型:期刊论文

作者Xiang, Jie1,2,3; Zhang, Songping4; Zhang, Guifeng4; Li, Xiunan4; Zhang, Chun1,2,3; Luo, Jian4; Yu, Rong1,2,3; Su, Zhiguo4
刊名JOURNAL OF CHROMATOGRAPHY A
出版日期2020-10-25
卷号1630页码:9
ISSN号0021-9673
关键词Cohn fraction V supernatant Dual-mode chromatography Ion exchange Affinity Ethanol-water solution
DOI10.1016/j.chroma.2020.461451
英文摘要Plasma fractionation industry is by far the largest protein pharmaceutical provider, but there are still some plasma components in its industrial waste liquid that have not been utilized. This study aimed to develop a simple and efficient method for plasma protein recovery from Cohn fraction V supernatant (FVS), an effluent containing about 40% ethanol. A new affinity chromatography medium was synthesized with a fatty acid ligand. When the medium was applied to recovery of human serum albumin (HSA) from FVS at physiological pH7.4, the process was unsuccessful due to substantial decrease in capacity in the presence of high ethanol concentration. Nevertheless, change of pH from 7.4 to 4.2 emerged an improved adsorption capacity. The carboxyl group of the ligand began to act as cationic ion exchange role. Both HSA and alpha 2HS-glycoprotein were adsorbed by the column, but alpha 2HS-glycoprotein could be eluted by increasing pH from 4.2 to 7.4, while HSA was retained by the column and could only be eluted by addition of fatty acid. Therefore, the adsorption of albumin under pH 4.2 is charge-induced affinity adsorption, not simple ion exchange. The so-called dual-mode adsorption depends not only on the chromatographic medium but also on the separated object and environment. HPSEC showed that the purity of recovered HSA was greater than 98%. Circular dichroism and fluorescence spectra were consistent with that of the commercial product. Furthermore, the measurement by isothermal titration calorimetry showed that the separated HSA still maintained the binding activities with the ligands of warfarin and naproxen. It is therefore possible to directly recover high-purity and high-quality human serum albumin from the effluent of plasma fractionation industry by one-step chromatography. (C) 2020 Published by Elsevier B.V.
WOS关键词LARGE-SCALE PRODUCTION ; HUMAN SYNOVIAL FLUID ; PROTEINS ; BINDING ; PURIFICATION ; LIGAND ; SEPARATION
资助项目National Key R&D Program of China[2016YFD050080 0] ; National Key R&D Program of China[2016YFD0500809] ; National Natural Science Foundation of China[21821005] ; National Natural Science Foundation of China[81773623]
WOS研究方向Biochemistry & Molecular Biology ; Chemistry
语种英语
出版者ELSEVIER
WOS记录号WOS:000576788800019
资助机构National Key R&D Program of China ; National Natural Science Foundation of China
源URL[http://ir.ipe.ac.cn/handle/122111/42357]  
专题中国科学院过程工程研究所
通讯作者Luo, Jian; Yu, Rong; Su, Zhiguo
作者单位1.Sichuan Univ, Sichuan Res Ctr Drug Precis Ind Technol, West China Sch Pharm, Chengdu 610041, Peoples R China
2.Sichuan Univ, Key Lab Drug Targeting & Drug Delivery Syst, Educ Minist, Sichuan Engn Lab Plant Sourced Drug, Chengdu 610041, Peoples R China
3.Sichuan Univ, West China Sch Pharm, Dept Biopharmaceut, Chengdu 610041, Peoples R China
4.Chinese Acad Sci, Inst Proc Engn, State Key Lab Biochem Engn, Beijing 100190, Peoples R China
推荐引用方式
GB/T 7714
Xiang, Jie,Zhang, Songping,Zhang, Guifeng,et al. Recovery of human serum albumin by dual-mode chromatography from the waste stream of Cohn fraction V supernatant[J]. JOURNAL OF CHROMATOGRAPHY A,2020,1630:9.
APA Xiang, Jie.,Zhang, Songping.,Zhang, Guifeng.,Li, Xiunan.,Zhang, Chun.,...&Su, Zhiguo.(2020).Recovery of human serum albumin by dual-mode chromatography from the waste stream of Cohn fraction V supernatant.JOURNAL OF CHROMATOGRAPHY A,1630,9.
MLA Xiang, Jie,et al."Recovery of human serum albumin by dual-mode chromatography from the waste stream of Cohn fraction V supernatant".JOURNAL OF CHROMATOGRAPHY A 1630(2020):9.

入库方式: OAI收割

来源:过程工程研究所

浏览0
下载0
收藏0
其他版本

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。