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High yield of recombinant human apolipoprotein A-I expressed in Pichia pastoris by using mixed-mode chromatography

dc.contributor.authorJANAKIRAMAN, V. N.
dc.contributor.authorNOUBHANI, A.
dc.contributor.authorVENKATARAMAN, K.
dc.contributor.authorVIJAYALAKSHMI, M.
dc.contributor.authorSANTARELLI, X.
dc.date.accessioned2020-09-03T07:56:15Z
dc.date.available2020-09-03T07:56:15Z
dc.date.issued2016
dc.identifier.issn1860-6768
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/10857
dc.description.abstractEnA vast majority of the cardioprotective properties exhibited by high-density lipoprotein (HDL) is mediated by its major protein component apolipoprotein A-I (ApoA1). In order to develop a simplified bioprocess for producing recombinant human apolipoprotein A-I (rhApoA1) in its near-native form, rhApoA1 was expressed without the use of an affinity tag in view of its potential therapeutic applications. Expressed in Pichia pastoris at expression levels of 58.2 mg ApoA1 per liter of culture in a reproducible manner, the target protein was purified by mixed-mode chromatography using Capto T MMC ligand with a purity and recovery of 84 and 68%, respectively. ApoA1 purification was scaled up to mixed-mode expanded bed adsorption chromatography to establish an 'on-line' process for the efficient capture of rhApoA1 directly from the P. pastoris expression broth. A polishing step using anion exchange chromatography enabled the recovery of ApoA1 up to 96% purity. Purified ApoA1 was identified and verified by RPLC-ESI-Q-TOF mass spectrometry. This two-step process would reduce processing times and therefore costs in comparison to the twelve-step procedure currently used for recovering rhApoA1 from P. pastoris.
dc.language.isoen
dc.title.enHigh yield of recombinant human apolipoprotein A-I expressed in Pichia pastoris by using mixed-mode chromatography
dc.typeArticle de revue
dc.identifier.doi10.1002/biot.201500245
dc.subject.halChimie/Matériaux
bordeaux.journalBiotechnology Journal
bordeaux.page117-126
bordeaux.volume11
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248*
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN, UMR 5248)
bordeaux.issue1
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionBordeaux INP
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