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Screening of Twelve Pea (Pisum sativum L.) Cultivars and Their Isolates Focusing on the Protein Characterization, Functionality, and Sensory Profiles
Pea protein concentrates and isolates are important raw materials for the production of plant-based food products. To select suitable peas (Pisum sativum L.) for protein extraction for further use as food ingredients, twelve different cultivars were subjected to isoelectric precipitation and spray d...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8065828/ https://www.ncbi.nlm.nih.gov/pubmed/33918162 http://dx.doi.org/10.3390/foods10040758 |
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author | García Arteaga, Verónica Kraus, Sonja Schott, Michael Muranyi, Isabel Schweiggert-Weisz, Ute Eisner, Peter |
author_facet | García Arteaga, Verónica Kraus, Sonja Schott, Michael Muranyi, Isabel Schweiggert-Weisz, Ute Eisner, Peter |
author_sort | García Arteaga, Verónica |
collection | PubMed |
description | Pea protein concentrates and isolates are important raw materials for the production of plant-based food products. To select suitable peas (Pisum sativum L.) for protein extraction for further use as food ingredients, twelve different cultivars were subjected to isoelectric precipitation and spray drying. Both the dehulled pea flours and protein isolates were characterized regarding their chemical composition and the isolates were analyzed for their functional properties, sensory profiles, and molecular weight distributions. Orchestra, Florida, Dolores, and RLPY cultivars showed the highest protein yields. The electrophoretic profiles were similar, indicating the presence of all main pea allergens in all isolates. The colors of the isolates were significantly different regarding lightness (L*) and red-green (a*) components. The largest particle size was shown by the isolate from Florida cultivar, whereas the lowest was from the RLPY isolate. At pH 7, protein solubility ranged from 40% to 62% and the emulsifying capacity ranged from 600 to 835 mL g(−1). The principal component analysis revealed similarities among certain pea cultivars regarding their physicochemical and functional properties. The sensory profile of the individual isolates was rather similar, with an exception of the pea-like and bitter attributes, which were significantly different among the isolates. |
format | Online Article Text |
id | pubmed-8065828 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-80658282021-04-25 Screening of Twelve Pea (Pisum sativum L.) Cultivars and Their Isolates Focusing on the Protein Characterization, Functionality, and Sensory Profiles García Arteaga, Verónica Kraus, Sonja Schott, Michael Muranyi, Isabel Schweiggert-Weisz, Ute Eisner, Peter Foods Article Pea protein concentrates and isolates are important raw materials for the production of plant-based food products. To select suitable peas (Pisum sativum L.) for protein extraction for further use as food ingredients, twelve different cultivars were subjected to isoelectric precipitation and spray drying. Both the dehulled pea flours and protein isolates were characterized regarding their chemical composition and the isolates were analyzed for their functional properties, sensory profiles, and molecular weight distributions. Orchestra, Florida, Dolores, and RLPY cultivars showed the highest protein yields. The electrophoretic profiles were similar, indicating the presence of all main pea allergens in all isolates. The colors of the isolates were significantly different regarding lightness (L*) and red-green (a*) components. The largest particle size was shown by the isolate from Florida cultivar, whereas the lowest was from the RLPY isolate. At pH 7, protein solubility ranged from 40% to 62% and the emulsifying capacity ranged from 600 to 835 mL g(−1). The principal component analysis revealed similarities among certain pea cultivars regarding their physicochemical and functional properties. The sensory profile of the individual isolates was rather similar, with an exception of the pea-like and bitter attributes, which were significantly different among the isolates. MDPI 2021-04-02 /pmc/articles/PMC8065828/ /pubmed/33918162 http://dx.doi.org/10.3390/foods10040758 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/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 (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article García Arteaga, Verónica Kraus, Sonja Schott, Michael Muranyi, Isabel Schweiggert-Weisz, Ute Eisner, Peter Screening of Twelve Pea (Pisum sativum L.) Cultivars and Their Isolates Focusing on the Protein Characterization, Functionality, and Sensory Profiles |
title | Screening of Twelve Pea (Pisum sativum L.) Cultivars and Their Isolates Focusing on the Protein Characterization, Functionality, and Sensory Profiles |
title_full | Screening of Twelve Pea (Pisum sativum L.) Cultivars and Their Isolates Focusing on the Protein Characterization, Functionality, and Sensory Profiles |
title_fullStr | Screening of Twelve Pea (Pisum sativum L.) Cultivars and Their Isolates Focusing on the Protein Characterization, Functionality, and Sensory Profiles |
title_full_unstemmed | Screening of Twelve Pea (Pisum sativum L.) Cultivars and Their Isolates Focusing on the Protein Characterization, Functionality, and Sensory Profiles |
title_short | Screening of Twelve Pea (Pisum sativum L.) Cultivars and Their Isolates Focusing on the Protein Characterization, Functionality, and Sensory Profiles |
title_sort | screening of twelve pea (pisum sativum l.) cultivars and their isolates focusing on the protein characterization, functionality, and sensory profiles |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8065828/ https://www.ncbi.nlm.nih.gov/pubmed/33918162 http://dx.doi.org/10.3390/foods10040758 |
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