Please use this identifier to cite or link to this item: http://hdl.handle.net/10773/28170
Title: Distinct roles of salt cations and anions upon the salting-out of electro-positive albumin
Author: Madeira, Pedro P.
Freire, Mara G.
Coutinho, João A. P.
Issue Date: 1-Mar-2020
Publisher: Elsevier
Abstract: Precipitation 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.
Peer review: yes
URI: http://hdl.handle.net/10773/28170
DOI: 10.1016/j.molliq.2019.112409
ISSN: 0167-7322
Appears in Collections:CICECO - Artigos

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