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Soy Protein Isolate/Sodium Alginate Microparticles under Different pH Conditions: Formation Mechanism and Physicochemical Properties
The effects of sodium alginate (SA) and pH value on the formation, structural properties, microscopic morphology, and physicochemical properties of soybean protein isolate (SPI)/SA microparticles were investigated. The results of ζ-potential and free sulfhydryl (SH) content showed electrostatic inte...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8947744/ https://www.ncbi.nlm.nih.gov/pubmed/35327213 http://dx.doi.org/10.3390/foods11060790 |
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author | Cao, Jia Tong, Xiaohong Wang, Mengmeng Tian, Tian Yang, Sai Sun, Mingyue Lyu, Bo Cao, Xinru Wang, Huan Jiang, Lianzhou |
author_facet | Cao, Jia Tong, Xiaohong Wang, Mengmeng Tian, Tian Yang, Sai Sun, Mingyue Lyu, Bo Cao, Xinru Wang, Huan Jiang, Lianzhou |
author_sort | Cao, Jia |
collection | PubMed |
description | The effects of sodium alginate (SA) and pH value on the formation, structural properties, microscopic morphology, and physicochemical properties of soybean protein isolate (SPI)/SA microparticles were investigated. The results of ζ-potential and free sulfhydryl (SH) content showed electrostatic interactions between SPI and SA, which promoted the conversion of free SH into disulfide bonds within the protein. The surface hydrophobicity, fluorescence spectra, and Fourier transform infrared spectroscopy data suggested that the secondary structure and microenvironment of the internal hydrophobic groups of the protein in the SPI/SA microparticles were changed. Compared with SPI microparticles, the surface of SPI/SA microparticles was smoother, the degree of collapse was reduced, and the thermal stability was improved. In addition, under the condition of pH 9.0, the average particle size of SPI/SA microparticles was only 15.92 ± 0.66 μm, and the distribution was uniform. Rheological tests indicated that SA significantly increased the apparent viscosity of SPI/SA microparticles at pH 9.0. The maximum protein solubility (67.32%), foaming ability (91.53 ± 1.12%), and emulsion activity (200.29 ± 3.38 m(2)/g) of SPI/SA microparticles occurred at pH 9.0. The application of SPI/SA microparticles as ingredients in high-protein foods is expected to be of great significance in the food industry. |
format | Online Article Text |
id | pubmed-8947744 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-89477442022-03-25 Soy Protein Isolate/Sodium Alginate Microparticles under Different pH Conditions: Formation Mechanism and Physicochemical Properties Cao, Jia Tong, Xiaohong Wang, Mengmeng Tian, Tian Yang, Sai Sun, Mingyue Lyu, Bo Cao, Xinru Wang, Huan Jiang, Lianzhou Foods Article The effects of sodium alginate (SA) and pH value on the formation, structural properties, microscopic morphology, and physicochemical properties of soybean protein isolate (SPI)/SA microparticles were investigated. The results of ζ-potential and free sulfhydryl (SH) content showed electrostatic interactions between SPI and SA, which promoted the conversion of free SH into disulfide bonds within the protein. The surface hydrophobicity, fluorescence spectra, and Fourier transform infrared spectroscopy data suggested that the secondary structure and microenvironment of the internal hydrophobic groups of the protein in the SPI/SA microparticles were changed. Compared with SPI microparticles, the surface of SPI/SA microparticles was smoother, the degree of collapse was reduced, and the thermal stability was improved. In addition, under the condition of pH 9.0, the average particle size of SPI/SA microparticles was only 15.92 ± 0.66 μm, and the distribution was uniform. Rheological tests indicated that SA significantly increased the apparent viscosity of SPI/SA microparticles at pH 9.0. The maximum protein solubility (67.32%), foaming ability (91.53 ± 1.12%), and emulsion activity (200.29 ± 3.38 m(2)/g) of SPI/SA microparticles occurred at pH 9.0. The application of SPI/SA microparticles as ingredients in high-protein foods is expected to be of great significance in the food industry. MDPI 2022-03-09 /pmc/articles/PMC8947744/ /pubmed/35327213 http://dx.doi.org/10.3390/foods11060790 Text en © 2022 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 Cao, Jia Tong, Xiaohong Wang, Mengmeng Tian, Tian Yang, Sai Sun, Mingyue Lyu, Bo Cao, Xinru Wang, Huan Jiang, Lianzhou Soy Protein Isolate/Sodium Alginate Microparticles under Different pH Conditions: Formation Mechanism and Physicochemical Properties |
title | Soy Protein Isolate/Sodium Alginate Microparticles under Different pH Conditions: Formation Mechanism and Physicochemical Properties |
title_full | Soy Protein Isolate/Sodium Alginate Microparticles under Different pH Conditions: Formation Mechanism and Physicochemical Properties |
title_fullStr | Soy Protein Isolate/Sodium Alginate Microparticles under Different pH Conditions: Formation Mechanism and Physicochemical Properties |
title_full_unstemmed | Soy Protein Isolate/Sodium Alginate Microparticles under Different pH Conditions: Formation Mechanism and Physicochemical Properties |
title_short | Soy Protein Isolate/Sodium Alginate Microparticles under Different pH Conditions: Formation Mechanism and Physicochemical Properties |
title_sort | soy protein isolate/sodium alginate microparticles under different ph conditions: formation mechanism and physicochemical properties |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8947744/ https://www.ncbi.nlm.nih.gov/pubmed/35327213 http://dx.doi.org/10.3390/foods11060790 |
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