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dc.contributor.authorMadeira, Pedro P.pt_PT
dc.contributor.authorFreire, Mara G.pt_PT
dc.contributor.authorCoutinho, João A. P.pt_PT
dc.description.abstractPrecipitation experiments of electro-positive albumin by the action of a wide number of salts, and at differentconcentrations, were performed at a constant temperature (25 °C). The pH range studied covered extreme acidicconditions up to hydronium concentrations where the dissociation of the protein carboxyl groups becomes no-ticeable. The time required for the clouding phenomenon to occur and the quantity of salted-out protein werealso ascertained. The results here reported show that the salt anion is the main salting-out species for the posi-tively charged protein, where their efficacy in salting-out albumin from aqueous solution increases in theorder: F−bCl−bBr−bNO3−bI−bSCN−~ ClO4−bSO42−. Although at extreme pH conditions the salt cationhas no significant influence on the protein salting-out, experiments performed at higher pH values, where thecarboxyl groups starts to dissociate, revealed a non-monotonic effect of the salt upon protein precipitation. Weinterpret this observation as a result of the presence of different protein forms, with which the salt cation partic-ipates in chemical equilibrium. Overall, the proteins salting-out phenomenon induced by salt can be rationalizedby a general mechanism driven by electrostatic interactions and chemical equilibrium concepts.pt_PT
dc.relationUniversity of Aveiro for funding in the scope of the framework contract fore-seen in the numbers 4, 5 and 6 of the article 23, of the Decree-Law 57/2016, of August 29, changed by Law 57/2017, of July 19.pt_PT
dc.titleDistinct roles of salt cations and anions upon the salting-out of electro-positive albuminpt_PT
degois.publication.titleJournal of Molecular Liquidspt_PT
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