Salt effects on the solubility of aromatic and dicarboxylic amino acids in water
Autor(a) principal: | |
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Data de Publicação: | 2023 |
Outros Autores: | , , , , , |
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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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 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier |
publisher.none.fl_str_mv |
Elsevier |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
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RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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1799137721630851072 |