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Salt effects on the solubility of aromatic and dicarboxylic amino acids in water

2023Journal article Open access
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dc.contributor.authorAliyeva, Mehriban
dc.contributor.authorBrandão, Paula
dc.contributor.authorGomes, José R.B.
dc.contributor.authorCoutinho, João A.P.
dc.contributor.authorHeld, Christoph
dc.contributor.authorFerreira, Olga
dc.contributor.authorPinho, Simão
dc.date.accessioned2023-05-29T15:39:35Z
dc.date.available2023-05-29T15:39:35Z
dc.date.issued2023
dc.description.abstractThe salt effect on the solubility of the amino acids L-aspartic acid, L-glutamic acid, L-tryptophan, and L-tyrosine, seldomly found in the literature, was studied at 298.2 K, in aqueous solutions of KCl and (NH4)2SO4, for salt concentrations up to 2.0 mol⋅kg -1. In this concentration range, both salts are salting-in agents for glutamic acid and aspartic acid, with a stronger effect induced by (NH4)2SO4. Regarding the two aromatic amino acids, a slight increase in the solubility was obtained at low salt concentrations, followed by a stronger salting-out effect, more pronounced by (NH4)2SO4 than by KCl. The relative solubility data obtained in this work were compared to literature data for other amino acids in the same electrolyte solutions to establish a relative solubility ranking connected to their structure. Finally, the solubility data were modeled using the electrolyte Perturbed-Chain Statistical Association Theory (ePC-SAFT). The modeling requires parameters for the amino acids and ions as well as melting properties of the amino acids. All these parameters and properties were obtained from previous works. To quantitatively describe the solubility of amino acids upon salt addition, binary interaction parameters (kij) between any amino acid and anions were determined, while between any amino acid and the cations were fixed to kij = 0.08. The kij parameters between amino acid and the inorganic anions show very similar values for amino acids of the same chemical class (e.g. kij between anion and amino acid with apolar side chains), which may be used to systematically reduce the number of adjustable parameters in future work.pt_PT
dc.description.sponsorshipThis work was developed within the scope of the project CIMOMountain Research Center, UIDB/00690/2020 and LA/P/0007/2020, and CICECO-Aveiro Institute of Materials, UIDB/50011/2020, UIDP/ 50011/2020 and LA/P/0006/2020, financed by national funds through the Portuguese Foundation for Science and Technology (FCT)/MCTES. Mehriban Aliyeva thanks FCT and European Social Fund (ESF) for her Ph.D. grant (SFRH/BD/139355/2018). The authors also thank Carina Silva for participating in the measurement of part of the solubility data.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationAliyeva, Mehriban; Brandão, Paula; Gomes, José R.B.; Coutinho, João A.P.; Held, Christoph; Ferreira, Olga; Pinho, Simão (2023). Salt effects on the solubility of aromatic and dicarboxylic amino acids in water. The Journal of Chemical Thermodynamics. ISSN 0021-9614. 177, p. 1-7pt_PT
dc.identifier.doi10.1016/j.jct.2022.106929pt_PT
dc.identifier.eissn1096-3626
dc.identifier.issn0021-9614
dc.identifier.urihttp://hdl.handle.net/10198/28395
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherElsevierpt_PT
dc.relationLA/P/0007/2020pt_PT
dc.relationMountain Research Center
dc.relationCICECO-Aveiro Institute of Materials
dc.relationCICECO-Aveiro Institute of Materials
dc.relationIon effects on Protein Model Compounds in Aqueous Systems: Experimental and Computational Studies
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectSolubilitypt_PT
dc.subjectAmino acidspt_PT
dc.subjectElectrolytespt_PT
dc.subjectePC-SAFTpt_PT
dc.subjectSalt effectpt_PT
dc.titleSalt effects on the solubility of aromatic and dicarboxylic amino acids in waterpt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleMountain Research Center
oaire.awardTitleCICECO-Aveiro Institute of Materials
oaire.awardTitleCICECO-Aveiro Institute of Materials
oaire.awardTitleIon effects on Protein Model Compounds in Aqueous Systems: Experimental and Computational Studies
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F00690%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F50011%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDP%2F50011%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/POR_CENTRO/SFRH%2FBD%2F139355%2F2018/PT
oaire.citation.startPage106929pt_PT
oaire.citation.titleThe Journal of Chemical Thermodynamicspt_PT
oaire.citation.volume177pt_PT
oaire.fundingStream6817 - DCRRNI ID
oaire.fundingStream6817 - DCRRNI ID
oaire.fundingStream6817 - DCRRNI ID
oaire.fundingStreamPOR_CENTRO
person.familyNameFerreira
person.familyNamePinho
person.givenNameOlga
person.givenNameSimão
person.identifier810882
person.identifier.ciencia-id9F1D-C75A-4A54
person.identifier.ciencia-id481D-73AD-8D0F
person.identifier.orcid0000-0001-8414-3479
person.identifier.orcid0000-0002-9211-857X
person.identifier.ridM-4567-2013
person.identifier.ridD-4148-2013
person.identifier.scopus-author-id57203083219
person.identifier.scopus-author-id7003570175
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
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