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Denaturation of inactivated FMDV in ion exchange chromatography: Evidence by differential scanning calorimetry analysis
Liang, Shanqin1,2; Yang, Yanli1; Sun, Lijing1; Zhao, Qizu3; Ma, Guanghui1; Zhang, Songping1; Su, Zhiguo1,4

Removing impurities by purification is important for livestock vaccines to avoid side effects and ensure sufficient immunogenic protection on animals. In this study, three anion-exchange media with similar particle size and ligand density except pore size were applied and compared for purification of inactivated foot-and-mouth disease virus (FMDV) antigen. The dynamic binding capacity for DEAE-POROS (214 nm) and DEAE-650 M (106 nm) were 11.53 and 10.03 mg/mL, while that for DEAE-FF (32 nm) was less than 1/10 df the previous two. The recovery of inactivated FMDV after chromatographic process of these three media was 68.42%, 66.32% and 54.46%, respectively, showing a decrement as the decrease of pore size of media. Possible denaturation of the FMDV on the surfaces of anion exchange media was analyzed by differential scanning calorimetry (DSC). FMDV is known to be prone to dissociate into smaller subunits 12S. In solution, this process is reflected by Tml of DSC, which is at about 48.52 degrees C. When inactivated FMDV were absorbed on DEAE-FF, the Tml became 41.73 degrees C, indicating the increased possibility of dissociation. The TO for DEAE-650 M and DEAE-POROS was 44.04 degrees C and 45.37 degrees C, showing less dissociation and imprdved stability than on DEAE-FF. After DEAE-POROS chromatography, 94% FMDV recovery with 7.7 fold purification was achieved, further polishing by size exclusion chromatography led totally 173-fold increase in purity with average overall recovery of 79%. (C) 2017 Elsevier B.V. All rights reserved.

KeywordFoot And Mouth Disease Virus Ion Exchange Chromatography Differential Scanning Calorimetry Stability Dissociation
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine ; Technology
Indexed BySCI
WOS KeywordMouth-disease Virus ; Size-exclusion Hplc ; Surface-antigen ; Particles ; Adsorption ; Protein ; Media ; Purification ; Vaccines ; Quantification
WOS Research AreaBiotechnology & Applied Microbiology ; Engineering
WOS SubjectBiotechnology & Applied Microbiology ; Engineering, Chemical
Funding OrganizationNatural Sciences Foundation of China(21336010 ; Special Fund for Agro-scientific Research in the Public Interest(201303046) ; National Key R D Program(2016YFD0500800) ; STS Grant from Chinese Academy of Sciences(KFJ-SW-STS-162) ; 21406239)
WOS IDWOS:000404199100012
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Cited Times:8[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
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
3.China Inst Vet Drug Control, Beijing 100081, Peoples R China
4.Jiangsu Natl Synerget Innovat Ctr Adv Mat, Nanjing 211800, Jiangsu, Peoples R China
Recommended Citation
GB/T 7714
Liang, Shanqin,Yang, Yanli,Sun, Lijing,et al. Denaturation of inactivated FMDV in ion exchange chromatography: Evidence by differential scanning calorimetry analysis[J]. BIOCHEMICAL ENGINEERING JOURNAL,2017,124:99-107.
APA Liang, Shanqin.,Yang, Yanli.,Sun, Lijing.,Zhao, Qizu.,Ma, Guanghui.,...&Su, Zhiguo.(2017).Denaturation of inactivated FMDV in ion exchange chromatography: Evidence by differential scanning calorimetry analysis.BIOCHEMICAL ENGINEERING JOURNAL,124,99-107.
MLA Liang, Shanqin,et al."Denaturation of inactivated FMDV in ion exchange chromatography: Evidence by differential scanning calorimetry analysis".BIOCHEMICAL ENGINEERING JOURNAL 124(2017):99-107.
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