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The Effect of High Pressure Homogenization on the Structure of Dual-Protein and Its Emulsion Functional Properties
It has been proven that high-pressure homogenization (HPH) could improve the functional properties of proteins by modifying their structure. This study researched the effect of HPH on the structural and functional properties of whey-soy dual-protein (Soy Protein Isolation-Whey Protein Isolation, SPI...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10529657/ https://www.ncbi.nlm.nih.gov/pubmed/37761067 http://dx.doi.org/10.3390/foods12183358 |
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author | Wu, Meishan He, Xiaoye Feng, Duo Li, Hu Han, Di Li, Qingye Zhao, Boya Li, Na Liu, Tianxin Wang, Jing |
author_facet | Wu, Meishan He, Xiaoye Feng, Duo Li, Hu Han, Di Li, Qingye Zhao, Boya Li, Na Liu, Tianxin Wang, Jing |
author_sort | Wu, Meishan |
collection | PubMed |
description | It has been proven that high-pressure homogenization (HPH) could improve the functional properties of proteins by modifying their structure. This study researched the effect of HPH on the structural and functional properties of whey-soy dual-protein (Soy Protein Isolation-Whey Protein Isolation, SPI-WPI). Different protein solution samples were treated with HPH at 30, 60, 90, 120 and 150 MPa, and the structure changed under different pressures was analyzed by measuring particle size, zeta potential, Fourier infrared spectrum (FTIR), fluorescence spectrum and scanning electron microscope (SEM). The results showed that HPH significantly reduced the particle size of SPI-WPI, changed the secondary and tertiary structures and improved the hydrophobic interaction between molecules. In addition, HPH significantly improved the solubility and emulsification of all proteins, and the improvement effect on SPI-WPI was significantly better than SPI and WPI. It was found that SPI-WPI treated with 60 MPa had the best physicochemical properties. Secondly, we researched the effect of HPH by 60 MPa on the emulsion properties of SPI-WPI. In this study, the SPI-WPI had the lowest surface tension compared to a single protein after HPH treatment. The emulsion droplet size was obviously decreased, and the elastic properties and physical stability of SPI-WPI emulsion were significantly enhanced. In conclusion, this study will provide a theoretical basis for the application of HPH in modifying the structure of dual-protein to improve its development and utilization in liquid specialty food. |
format | Online Article Text |
id | pubmed-10529657 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-105296572023-09-28 The Effect of High Pressure Homogenization on the Structure of Dual-Protein and Its Emulsion Functional Properties Wu, Meishan He, Xiaoye Feng, Duo Li, Hu Han, Di Li, Qingye Zhao, Boya Li, Na Liu, Tianxin Wang, Jing Foods Article It has been proven that high-pressure homogenization (HPH) could improve the functional properties of proteins by modifying their structure. This study researched the effect of HPH on the structural and functional properties of whey-soy dual-protein (Soy Protein Isolation-Whey Protein Isolation, SPI-WPI). Different protein solution samples were treated with HPH at 30, 60, 90, 120 and 150 MPa, and the structure changed under different pressures was analyzed by measuring particle size, zeta potential, Fourier infrared spectrum (FTIR), fluorescence spectrum and scanning electron microscope (SEM). The results showed that HPH significantly reduced the particle size of SPI-WPI, changed the secondary and tertiary structures and improved the hydrophobic interaction between molecules. In addition, HPH significantly improved the solubility and emulsification of all proteins, and the improvement effect on SPI-WPI was significantly better than SPI and WPI. It was found that SPI-WPI treated with 60 MPa had the best physicochemical properties. Secondly, we researched the effect of HPH by 60 MPa on the emulsion properties of SPI-WPI. In this study, the SPI-WPI had the lowest surface tension compared to a single protein after HPH treatment. The emulsion droplet size was obviously decreased, and the elastic properties and physical stability of SPI-WPI emulsion were significantly enhanced. In conclusion, this study will provide a theoretical basis for the application of HPH in modifying the structure of dual-protein to improve its development and utilization in liquid specialty food. MDPI 2023-09-07 /pmc/articles/PMC10529657/ /pubmed/37761067 http://dx.doi.org/10.3390/foods12183358 Text en © 2023 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 Wu, Meishan He, Xiaoye Feng, Duo Li, Hu Han, Di Li, Qingye Zhao, Boya Li, Na Liu, Tianxin Wang, Jing The Effect of High Pressure Homogenization on the Structure of Dual-Protein and Its Emulsion Functional Properties |
title | The Effect of High Pressure Homogenization on the Structure of Dual-Protein and Its Emulsion Functional Properties |
title_full | The Effect of High Pressure Homogenization on the Structure of Dual-Protein and Its Emulsion Functional Properties |
title_fullStr | The Effect of High Pressure Homogenization on the Structure of Dual-Protein and Its Emulsion Functional Properties |
title_full_unstemmed | The Effect of High Pressure Homogenization on the Structure of Dual-Protein and Its Emulsion Functional Properties |
title_short | The Effect of High Pressure Homogenization on the Structure of Dual-Protein and Its Emulsion Functional Properties |
title_sort | effect of high pressure homogenization on the structure of dual-protein and its emulsion functional properties |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10529657/ https://www.ncbi.nlm.nih.gov/pubmed/37761067 http://dx.doi.org/10.3390/foods12183358 |
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