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Functional and Rheological Properties of Vicia faba L. Protein Isolates

A protein isolate (85.5%) was obtained from the Vicia faba L. seeds. The main protein fraction, typical for the seeds of this plant, was found to be most numerous: Legumin (35 kDa) and Vicilin (45 kDa). The hydrodynamic and surface properties of isolate aqueous solutions were studied with the help o...

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Autores principales: Żmudziński, Daniel, Goik, Urszula, Ptaszek, Paweł
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7911567/
https://www.ncbi.nlm.nih.gov/pubmed/33525520
http://dx.doi.org/10.3390/biom11020178
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author Żmudziński, Daniel
Goik, Urszula
Ptaszek, Paweł
author_facet Żmudziński, Daniel
Goik, Urszula
Ptaszek, Paweł
author_sort Żmudziński, Daniel
collection PubMed
description A protein isolate (85.5%) was obtained from the Vicia faba L. seeds. The main protein fraction, typical for the seeds of this plant, was found to be most numerous: Legumin (35 kDa) and Vicilin (45 kDa). The hydrodynamic and surface properties of isolate aqueous solutions were studied with the help of dynamic light scattering, [Formula: see text]-potential, and tensometry in a wide range of concentrations and pH conditions. Selected functional properties, like foaming and emulsifying abilities, were studied. An increase of water solubility was shown with a raising pH, as well as a water holding capacity (WHC). The protein isolate showed a tendency to decrease the surface tension of water solutions, with high hydrophobicity and a negative charge of the isolate enhancing the foaming and emulsifying properties. The analysis of the concentration and the pH influence on selected functional properties indicated alkaline conditions as favorable for good foaming and emulsifying properties of the isolate and affected on their rheological properties.
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spelling pubmed-79115672021-02-28 Functional and Rheological Properties of Vicia faba L. Protein Isolates Żmudziński, Daniel Goik, Urszula Ptaszek, Paweł Biomolecules Article A protein isolate (85.5%) was obtained from the Vicia faba L. seeds. The main protein fraction, typical for the seeds of this plant, was found to be most numerous: Legumin (35 kDa) and Vicilin (45 kDa). The hydrodynamic and surface properties of isolate aqueous solutions were studied with the help of dynamic light scattering, [Formula: see text]-potential, and tensometry in a wide range of concentrations and pH conditions. Selected functional properties, like foaming and emulsifying abilities, were studied. An increase of water solubility was shown with a raising pH, as well as a water holding capacity (WHC). The protein isolate showed a tendency to decrease the surface tension of water solutions, with high hydrophobicity and a negative charge of the isolate enhancing the foaming and emulsifying properties. The analysis of the concentration and the pH influence on selected functional properties indicated alkaline conditions as favorable for good foaming and emulsifying properties of the isolate and affected on their rheological properties. MDPI 2021-01-28 /pmc/articles/PMC7911567/ /pubmed/33525520 http://dx.doi.org/10.3390/biom11020178 Text en © 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Żmudziński, Daniel
Goik, Urszula
Ptaszek, Paweł
Functional and Rheological Properties of Vicia faba L. Protein Isolates
title Functional and Rheological Properties of Vicia faba L. Protein Isolates
title_full Functional and Rheological Properties of Vicia faba L. Protein Isolates
title_fullStr Functional and Rheological Properties of Vicia faba L. Protein Isolates
title_full_unstemmed Functional and Rheological Properties of Vicia faba L. Protein Isolates
title_short Functional and Rheological Properties of Vicia faba L. Protein Isolates
title_sort functional and rheological properties of vicia faba l. protein isolates
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7911567/
https://www.ncbi.nlm.nih.gov/pubmed/33525520
http://dx.doi.org/10.3390/biom11020178
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