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

Detalhes bibliográficos
Autor(a) principal: Aliyeva, Mehriban
Data de Publicação: 2023
Outros Autores: Brandão, Paula, Gomes, José R. B., Coutinho, João A. P., Held, Christoph, Ferreira, Olga, Pinho, Simão P.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10773/35855
Resumo: The 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.
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spelling Salt effects on the solubility of aromatic and dicarboxylic amino acids in waterSolubilityAmino acidsElectrolytesePC-SAFTSalt effectThe 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.Elsevier2023-01-18T15:11:14Z2023-02-01T00:00:00Z2023-02info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10773/35855eng0021-961410.1016/j.jct.2022.106929Aliyeva, MehribanBrandão, PaulaGomes, José R. B.Coutinho, João A. P.Held, ChristophFerreira, OlgaPinho, Simão P.info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-02-22T12:08:37Zoai:ria.ua.pt:10773/35855Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:06:36.362835Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Salt effects on the solubility of aromatic and dicarboxylic amino acids in water
title Salt effects on the solubility of aromatic and dicarboxylic amino acids in water
spellingShingle Salt effects on the solubility of aromatic and dicarboxylic amino acids in water
Aliyeva, Mehriban
Solubility
Amino acids
Electrolytes
ePC-SAFT
Salt effect
title_short Salt effects on the solubility of aromatic and dicarboxylic amino acids in water
title_full Salt effects on the solubility of aromatic and dicarboxylic amino acids in water
title_fullStr Salt effects on the solubility of aromatic and dicarboxylic amino acids in water
title_full_unstemmed Salt effects on the solubility of aromatic and dicarboxylic amino acids in water
title_sort Salt effects on the solubility of aromatic and dicarboxylic amino acids in water
author Aliyeva, Mehriban
author_facet Aliyeva, Mehriban
Brandão, Paula
Gomes, José R. B.
Coutinho, João A. P.
Held, Christoph
Ferreira, Olga
Pinho, Simão P.
author_role author
author2 Brandão, Paula
Gomes, José R. B.
Coutinho, João A. P.
Held, Christoph
Ferreira, Olga
Pinho, Simão P.
author2_role author
author
author
author
author
author
dc.contributor.author.fl_str_mv Aliyeva, Mehriban
Brandão, Paula
Gomes, José R. B.
Coutinho, João A. P.
Held, Christoph
Ferreira, Olga
Pinho, Simão P.
dc.subject.por.fl_str_mv Solubility
Amino acids
Electrolytes
ePC-SAFT
Salt effect
topic Solubility
Amino acids
Electrolytes
ePC-SAFT
Salt effect
description The 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.
publishDate 2023
dc.date.none.fl_str_mv 2023-01-18T15:11:14Z
2023-02-01T00:00:00Z
2023-02
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10773/35855
url http://hdl.handle.net/10773/35855
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0021-9614
10.1016/j.jct.2022.106929
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dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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