Structural Study of Wheat Gliadin in Different Solvents by Spectroscopic Techniques
Autor(a) principal: | |
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Data de Publicação: | 2021 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Journal of the Brazilian Chemical Society (Online) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532021000400695 |
Resumo: | Physicochemical properties of gliadin in different solvents (dimethyl sulfoxide (DMSO), H2O, and aqueous ethanol) and pH (9.8, 6.8, and 1.2) were investigated using dynamic light scattering (DLS), zeta potential (ZP), and attenuated total reflectance Fourier transform infrared spectroscopy (ATR-FTIR). Gliadin-DMSO and gliadin-deionized water (H2O) (pH 9.8) showed a lower size distribution, whereas samples solubilized in 60% aqueous ethanol presented a lower size distribution only at pH 1.2. ZP analysis showed that gliadin-H2O (pH 9.8) was the most stable evaluated system. ZP results of gliadin-DMSO indicated an unstable system, with the coexistence of several protein conformations. ATR-FTIR analysis showed that, in H2O, most protein conformations were β-sheets, while in DMSO a band at 1660 cm−1 appeared to be related to protein unfolding. The techniques proved to be effective in monitoring conformation and stability of all gliadin/solvent systems. Such information can be used in the development of new gliadin-based materials. |
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Structural Study of Wheat Gliadin in Different Solvents by Spectroscopic TechniquesgliadinspectroscopymorphologystabilitybiotechnologyPhysicochemical properties of gliadin in different solvents (dimethyl sulfoxide (DMSO), H2O, and aqueous ethanol) and pH (9.8, 6.8, and 1.2) were investigated using dynamic light scattering (DLS), zeta potential (ZP), and attenuated total reflectance Fourier transform infrared spectroscopy (ATR-FTIR). Gliadin-DMSO and gliadin-deionized water (H2O) (pH 9.8) showed a lower size distribution, whereas samples solubilized in 60% aqueous ethanol presented a lower size distribution only at pH 1.2. ZP analysis showed that gliadin-H2O (pH 9.8) was the most stable evaluated system. ZP results of gliadin-DMSO indicated an unstable system, with the coexistence of several protein conformations. ATR-FTIR analysis showed that, in H2O, most protein conformations were β-sheets, while in DMSO a band at 1660 cm−1 appeared to be related to protein unfolding. The techniques proved to be effective in monitoring conformation and stability of all gliadin/solvent systems. Such information can be used in the development of new gliadin-based materials.Sociedade Brasileira de Química2021-04-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532021000400695Journal of the Brazilian Chemical Society v.32 n.4 2021reponame:Journal of the Brazilian Chemical Society (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.21577/0103-5053.20200221info:eu-repo/semantics/openAccessRibeiro,Andresa C.Leite,Daiani C.Scheibel,Jóice M.Soares,Rosane M. D.Silveira,Nádya P.eng2021-03-25T00:00:00Zoai:scielo:S0103-50532021000400695Revistahttp://jbcs.sbq.org.brONGhttps://old.scielo.br/oai/scielo-oai.php||office@jbcs.sbq.org.br1678-47900103-5053opendoar:2021-03-25T00:00Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ)false |
dc.title.none.fl_str_mv |
Structural Study of Wheat Gliadin in Different Solvents by Spectroscopic Techniques |
title |
Structural Study of Wheat Gliadin in Different Solvents by Spectroscopic Techniques |
spellingShingle |
Structural Study of Wheat Gliadin in Different Solvents by Spectroscopic Techniques Ribeiro,Andresa C. gliadin spectroscopy morphology stability biotechnology |
title_short |
Structural Study of Wheat Gliadin in Different Solvents by Spectroscopic Techniques |
title_full |
Structural Study of Wheat Gliadin in Different Solvents by Spectroscopic Techniques |
title_fullStr |
Structural Study of Wheat Gliadin in Different Solvents by Spectroscopic Techniques |
title_full_unstemmed |
Structural Study of Wheat Gliadin in Different Solvents by Spectroscopic Techniques |
title_sort |
Structural Study of Wheat Gliadin in Different Solvents by Spectroscopic Techniques |
author |
Ribeiro,Andresa C. |
author_facet |
Ribeiro,Andresa C. Leite,Daiani C. Scheibel,Jóice M. Soares,Rosane M. D. Silveira,Nádya P. |
author_role |
author |
author2 |
Leite,Daiani C. Scheibel,Jóice M. Soares,Rosane M. D. Silveira,Nádya P. |
author2_role |
author author author author |
dc.contributor.author.fl_str_mv |
Ribeiro,Andresa C. Leite,Daiani C. Scheibel,Jóice M. Soares,Rosane M. D. Silveira,Nádya P. |
dc.subject.por.fl_str_mv |
gliadin spectroscopy morphology stability biotechnology |
topic |
gliadin spectroscopy morphology stability biotechnology |
description |
Physicochemical properties of gliadin in different solvents (dimethyl sulfoxide (DMSO), H2O, and aqueous ethanol) and pH (9.8, 6.8, and 1.2) were investigated using dynamic light scattering (DLS), zeta potential (ZP), and attenuated total reflectance Fourier transform infrared spectroscopy (ATR-FTIR). Gliadin-DMSO and gliadin-deionized water (H2O) (pH 9.8) showed a lower size distribution, whereas samples solubilized in 60% aqueous ethanol presented a lower size distribution only at pH 1.2. ZP analysis showed that gliadin-H2O (pH 9.8) was the most stable evaluated system. ZP results of gliadin-DMSO indicated an unstable system, with the coexistence of several protein conformations. ATR-FTIR analysis showed that, in H2O, most protein conformations were β-sheets, while in DMSO a band at 1660 cm−1 appeared to be related to protein unfolding. The techniques proved to be effective in monitoring conformation and stability of all gliadin/solvent systems. Such information can be used in the development of new gliadin-based materials. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-04-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532021000400695 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532021000400695 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.21577/0103-5053.20200221 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Sociedade Brasileira de Química |
publisher.none.fl_str_mv |
Sociedade Brasileira de Química |
dc.source.none.fl_str_mv |
Journal of the Brazilian Chemical Society v.32 n.4 2021 reponame:Journal of the Brazilian Chemical Society (Online) instname:Sociedade Brasileira de Química (SBQ) instacron:SBQ |
instname_str |
Sociedade Brasileira de Química (SBQ) |
instacron_str |
SBQ |
institution |
SBQ |
reponame_str |
Journal of the Brazilian Chemical Society (Online) |
collection |
Journal of the Brazilian Chemical Society (Online) |
repository.name.fl_str_mv |
Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ) |
repository.mail.fl_str_mv |
||office@jbcs.sbq.org.br |
_version_ |
1750318183974174720 |