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Functional, textural, and rheological properties of mixed casein micelle and pea protein isolate co-dispersions
In the midst of rising consumer health and environmental concerns, pea protein has increased in popularity as an alternative to animal-origin proteins. However, the use of pea protein in food systems is largely hindered by its poor functionality, including low solubility. The objective of this study...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9623808/ https://www.ncbi.nlm.nih.gov/pubmed/36339743 http://dx.doi.org/10.3168/jdsc.2021-0157 |
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author | Krentz, Abigail García-Cano, Israel Jiménez-Flores, Rafael |
author_facet | Krentz, Abigail García-Cano, Israel Jiménez-Flores, Rafael |
author_sort | Krentz, Abigail |
collection | PubMed |
description | In the midst of rising consumer health and environmental concerns, pea protein has increased in popularity as an alternative to animal-origin proteins. However, the use of pea protein in food systems is largely hindered by its poor functionality, including low solubility. The objective of this study was to measure the textural, functional, and rheological properties of a mixed plant- and animal-based protein system. Caseins, the major protein in bovine milk, are a known animal-based protein with optimal functional properties and high sensory acceptability. Through cold-temperature homogenization, insoluble pea proteins were incorporated with casein micelles in a stable, mixed, colloidal dispersion. Three blends with various casein-to-pea ratios (90:10, 80:20, 50:50) were prepared and analyzed. We hypothesized that incorporation with casein micelles would improve the poor functional properties of pea protein, and thus increase its potential uses in the food industry as a functional ingredient. The protein blend successfully underwent chymosin coagulation, a key ability of caseins, and formed protein gels with textures similar to commercial queso fresco and hard tofu. The 50% casein micelle:50% pea protein blend had better emulsification properties than pea protein alone. In contrast, this blend had the same foaming properties as pea protein alone. The mixed protein blends had similar rheological properties to skim milk, thus increasing their potential applications in the food industry. These results serve as a starting point to begin fully understanding the interactions between pea protein isolate and casein micelles combined via low-temperature homogenization and the effect on their techno-functional properties. |
format | Online Article Text |
id | pubmed-9623808 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-96238082022-11-04 Functional, textural, and rheological properties of mixed casein micelle and pea protein isolate co-dispersions Krentz, Abigail García-Cano, Israel Jiménez-Flores, Rafael JDS Commun Dairy Foods In the midst of rising consumer health and environmental concerns, pea protein has increased in popularity as an alternative to animal-origin proteins. However, the use of pea protein in food systems is largely hindered by its poor functionality, including low solubility. The objective of this study was to measure the textural, functional, and rheological properties of a mixed plant- and animal-based protein system. Caseins, the major protein in bovine milk, are a known animal-based protein with optimal functional properties and high sensory acceptability. Through cold-temperature homogenization, insoluble pea proteins were incorporated with casein micelles in a stable, mixed, colloidal dispersion. Three blends with various casein-to-pea ratios (90:10, 80:20, 50:50) were prepared and analyzed. We hypothesized that incorporation with casein micelles would improve the poor functional properties of pea protein, and thus increase its potential uses in the food industry as a functional ingredient. The protein blend successfully underwent chymosin coagulation, a key ability of caseins, and formed protein gels with textures similar to commercial queso fresco and hard tofu. The 50% casein micelle:50% pea protein blend had better emulsification properties than pea protein alone. In contrast, this blend had the same foaming properties as pea protein alone. The mixed protein blends had similar rheological properties to skim milk, thus increasing their potential applications in the food industry. These results serve as a starting point to begin fully understanding the interactions between pea protein isolate and casein micelles combined via low-temperature homogenization and the effect on their techno-functional properties. Elsevier 2022-02-10 /pmc/articles/PMC9623808/ /pubmed/36339743 http://dx.doi.org/10.3168/jdsc.2021-0157 Text en © 2022. https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Dairy Foods Krentz, Abigail García-Cano, Israel Jiménez-Flores, Rafael Functional, textural, and rheological properties of mixed casein micelle and pea protein isolate co-dispersions |
title | Functional, textural, and rheological properties of mixed casein micelle and pea protein isolate co-dispersions |
title_full | Functional, textural, and rheological properties of mixed casein micelle and pea protein isolate co-dispersions |
title_fullStr | Functional, textural, and rheological properties of mixed casein micelle and pea protein isolate co-dispersions |
title_full_unstemmed | Functional, textural, and rheological properties of mixed casein micelle and pea protein isolate co-dispersions |
title_short | Functional, textural, and rheological properties of mixed casein micelle and pea protein isolate co-dispersions |
title_sort | functional, textural, and rheological properties of mixed casein micelle and pea protein isolate co-dispersions |
topic | Dairy Foods |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9623808/ https://www.ncbi.nlm.nih.gov/pubmed/36339743 http://dx.doi.org/10.3168/jdsc.2021-0157 |
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