Physicochemical and structural properties of major protein fractions of two varieties of nea-cowpea (vigna unguiculata l.): a comparative study

In both cowpea varieties, the globulin was the major protein fraction followed by albumins, glutelins and prolamins with 48 ± 2 g/100 g, 33 ± 2 g/100 g, 8 ± 1 g/100 g and 2 ± 0.5 g/100 g of the total seed protein content, respectively. Under non-reducing conditions, the CU and CO globulin fractions,...

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Autores principales: Avanza, María Victoria, Acevedo, Belén Andrea, Chaves, María Guadalupe, Aphalo, Paula, Añón, María Cristina
Formato: Artículo
Lenguaje:Inglés
Publicado: International Association of Food and Nutrition Scientists 2021
Materias:
Albumin
Globulin
Thermal properties
Surface hydrophobicity
Acceso en línea:http://repositorio.unne.edu.ar/handle/123456789/28257
Aporte de:
RIUNNE - Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE) de Universidad Nacional del Nordeste
id I48-R184-123456789-28257
record_format dspace
spelling I48-R184-123456789-282572025-03-06T10:58:01Z Physicochemical and structural properties of major protein fractions of two varieties of nea-cowpea (vigna unguiculata l.): a comparative study Avanza, María Victoria Acevedo, Belén Andrea Chaves, María Guadalupe Aphalo, Paula Añón, María Cristina Albumin Globulin Thermal properties Surface hydrophobicity In both cowpea varieties, the globulin was the major protein fraction followed by albumins, glutelins and prolamins with 48 ± 2 g/100 g, 33 ± 2 g/100 g, 8 ± 1 g/100 g and 2 ± 0.5 g/100 g of the total seed protein content, respectively. Under non-reducing conditions, the CU and CO globulin fractions, showed four major polypeptides with molecular masses of 80 ± 3, 65 ± 3, 56 ± 2 and 52 ± 2 kDa and some polypeptides with molecular masses ranging 45-25 kDa. Albumin and globulin fractions of CU showed the lowest values of enthalpy (H) suggesting an initial partial denaturation. Globulin fraction showed a higher content of aromatic amino acids than the albumin fraction, displaying a more hydrophobic behaviour. Results provide useful data that will be supplemented with further studies on functional properties of these proteins fractions, followed by the development of legume protein products. 2021-07-08T13:23:06Z 2021-07-08T13:23:06Z 2015-09 Artículo Avanza, María Victoria, et al., 2015. Physicochemical and structural properties of major protein fractions of two varieties of nea-cowpea (vigna unguiculata l.): a comparative study. International journal of food and nutritional sciences. New Delhi: International Association of Food and Nutrition Scientists, vol. 4, no. 4, p. 240-247. ISSN 2320-7876. http://repositorio.unne.edu.ar/handle/123456789/28257 eng openAccess http://creativecommons.org/licenses/by-nc-nd/2.5/ar/ application/pdf application/pdf International Association of Food and Nutrition Scientists International journal of food and nutritional sciences, vol. 4, no. 4, p. 240-247.
institution Universidad Nacional del Nordeste
institution_str I-48
repository_str R-184
collection RIUNNE - Repositorio Institucional de la Universidad Nacional del Nordeste (UNNE)
language Inglés
topic Albumin
Globulin
Thermal properties
Surface hydrophobicity
spellingShingle Albumin
Globulin
Thermal properties
Surface hydrophobicity
Avanza, María Victoria
Acevedo, Belén Andrea
Chaves, María Guadalupe
Aphalo, Paula
Añón, María Cristina
Physicochemical and structural properties of major protein fractions of two varieties of nea-cowpea (vigna unguiculata l.): a comparative study
topic_facet Albumin
Globulin
Thermal properties
Surface hydrophobicity
description In both cowpea varieties, the globulin was the major protein fraction followed by albumins, glutelins and prolamins with 48 ± 2 g/100 g, 33 ± 2 g/100 g, 8 ± 1 g/100 g and 2 ± 0.5 g/100 g of the total seed protein content, respectively. Under non-reducing conditions, the CU and CO globulin fractions, showed four major polypeptides with molecular masses of 80 ± 3, 65 ± 3, 56 ± 2 and 52 ± 2 kDa and some polypeptides with molecular masses ranging 45-25 kDa. Albumin and globulin fractions of CU showed the lowest values of enthalpy (H) suggesting an initial partial denaturation. Globulin fraction showed a higher content of aromatic amino acids than the albumin fraction, displaying a more hydrophobic behaviour. Results provide useful data that will be supplemented with further studies on functional properties of these proteins fractions, followed by the development of legume protein products.
format Artículo
author Avanza, María Victoria
Acevedo, Belén Andrea
Chaves, María Guadalupe
Aphalo, Paula
Añón, María Cristina
author_facet Avanza, María Victoria
Acevedo, Belén Andrea
Chaves, María Guadalupe
Aphalo, Paula
Añón, María Cristina
author_sort Avanza, María Victoria
title Physicochemical and structural properties of major protein fractions of two varieties of nea-cowpea (vigna unguiculata l.): a comparative study
title_short Physicochemical and structural properties of major protein fractions of two varieties of nea-cowpea (vigna unguiculata l.): a comparative study
title_full Physicochemical and structural properties of major protein fractions of two varieties of nea-cowpea (vigna unguiculata l.): a comparative study
title_fullStr Physicochemical and structural properties of major protein fractions of two varieties of nea-cowpea (vigna unguiculata l.): a comparative study
title_full_unstemmed Physicochemical and structural properties of major protein fractions of two varieties of nea-cowpea (vigna unguiculata l.): a comparative study
title_sort physicochemical and structural properties of major protein fractions of two varieties of nea-cowpea (vigna unguiculata l.): a comparative study
publisher International Association of Food and Nutrition Scientists
publishDate 2021
url http://repositorio.unne.edu.ar/handle/123456789/28257
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