Structural characterization of protein isolates obtained from chia (Salvia hispanica L.) seeds

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Abstract: Chia protein isolates (CPI) were obtained through isoelectric precipitation under two different conditions in order to compare their structural properties. Extraction was carried out at pH 10 or 12, whereas precipitation pH was fixed at 4.5. Samples were named as CPI10 or CPI12, according...

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Autores principales: López, Débora Natalia, Ingrassia, Romina, Busti, Pablo, Bonino, Julia, Delgado, Juan Francisco, Wagner, Jorge, Boeris, Valeria, Spelzini, Darío
Formato: Artículo
Lenguaje:Inglés
Publicado: Elsevier 2020
Materias:
CHIA
PROTEINAS VEGETALES
INDUSTRIA ALIMENTARIA
Acceso en línea:https://repositorio.uca.edu.ar/handle/123456789/9497
Aporte de:
Repositorio Institucional de la Universidad Católica Argentina (UCA) de Universidad Católica Argentina
id I33-R139123456789-9497
record_format dspace
institution Universidad Católica Argentina
institution_str I-33
repository_str R-139
collection Repositorio Institucional de la Universidad Católica Argentina (UCA)
language Inglés
topic CHIA
PROTEINAS VEGETALES
INDUSTRIA ALIMENTARIA
spellingShingle CHIA
PROTEINAS VEGETALES
INDUSTRIA ALIMENTARIA
López, Débora Natalia
Ingrassia, Romina
Busti, Pablo
Bonino, Julia
Delgado, Juan Francisco
Wagner, Jorge
Boeris, Valeria
Spelzini, Darío
Structural characterization of protein isolates obtained from chia (Salvia hispanica L.) seeds
topic_facet CHIA
PROTEINAS VEGETALES
INDUSTRIA ALIMENTARIA
description Abstract: Chia protein isolates (CPI) were obtained through isoelectric precipitation under two different conditions in order to compare their structural properties. Extraction was carried out at pH 10 or 12, whereas precipitation pH was fixed at 4.5. Samples were named as CPI10 or CPI12, according to their extraction pH (10 or 12, respectively). The recovery of chia proteins was higher when the extraction was carried out at pH 12 (17% for CPI12 and 13% for CPI10); however, CPI12 protein content (775  g/kg) was slightly lower than CPI10 protein content (782  g/kg). Both samples showed similar SDS-PAGE pattern. Protein dispersions of both isolates led to highly stabilized particles due to their negative ζ potential (around −54 mV). CPI10 has a higher proportion of small particles in suspension, revealed by a lower d3,2 value. Spectroscopic techniques showed that CPI10 presented higher content of β-helix than CPI12, resulting in higher thermal stability. This observation was supported by FT-IR spectroscopy since CPI10 presented less unordered structure than CPI12. The energy of endotherms obtained in CPI12 was considerably lower than in CPI10. Extraction at higher alkaline conditions led to a more denatured protein conformation with a higher content of random structure (18.1% for CPI10 and 22.9% for CPI12).
format Artículo
author López, Débora Natalia
Ingrassia, Romina
Busti, Pablo
Bonino, Julia
Delgado, Juan Francisco
Wagner, Jorge
Boeris, Valeria
Spelzini, Darío
author_facet López, Débora Natalia
Ingrassia, Romina
Busti, Pablo
Bonino, Julia
Delgado, Juan Francisco
Wagner, Jorge
Boeris, Valeria
Spelzini, Darío
author_sort López, Débora Natalia
title Structural characterization of protein isolates obtained from chia (Salvia hispanica L.) seeds
title_short Structural characterization of protein isolates obtained from chia (Salvia hispanica L.) seeds
title_full Structural characterization of protein isolates obtained from chia (Salvia hispanica L.) seeds
title_fullStr Structural characterization of protein isolates obtained from chia (Salvia hispanica L.) seeds
title_full_unstemmed Structural characterization of protein isolates obtained from chia (Salvia hispanica L.) seeds
title_sort structural characterization of protein isolates obtained from chia (salvia hispanica l.) seeds
publisher Elsevier
publishDate 2020
url https://repositorio.uca.edu.ar/handle/123456789/9497
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bdutipo_str Repositorios
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