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Formation of soybean protein isolate-hawthorn flavonoids non-covalent complexes: Linking the physicochemical properties and emulsifying properties
In recent years, more and more attention had been paid to the combination of proteins and flavonoids, and several flavonoids had been reported to improve the physicochemical and emulsifying properties of proteins. This study investigated the effects of ultrasonic treatment (450 W for 10 min, 20 min,...
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/PMC8892216/ https://www.ncbi.nlm.nih.gov/pubmed/35245861 http://dx.doi.org/10.1016/j.ultsonch.2022.105961 |
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author | Wang, Yi-Lun Yang, Jin-Jie Dai, Shi-Cheng Tong, Xiao-Hong Tian, Tian Liang, Chu-Chen Li, Liang Wang, Huan Jiang, Lian-Zhou |
author_facet | Wang, Yi-Lun Yang, Jin-Jie Dai, Shi-Cheng Tong, Xiao-Hong Tian, Tian Liang, Chu-Chen Li, Liang Wang, Huan Jiang, Lian-Zhou |
author_sort | Wang, Yi-Lun |
collection | PubMed |
description | In recent years, more and more attention had been paid to the combination of proteins and flavonoids, and several flavonoids had been reported to improve the physicochemical and emulsifying properties of proteins. This study investigated the effects of ultrasonic treatment (450 W for 10 min, 20 min, and 30 min) on the physicochemical properties, antioxidant activity, and emulsifying properties of soy protein isolate (SPI) -hawthorn flavonoids (HF) non-covalent complexes. The results showed that the addition of HF to SPI and 20 min of ultrasound could reduce α-helix and random coil, increase β-sheet and β-turn, and enhance fluorescence quenching. In addition, it decreased the particle size, zeta potential, surface hydrophobicity, and turbidity to 88.43 or 95.27 nm, −28.80 mV, 1250.42, and 0.23, respectively. The protein solubility, free sulfhydryl group, antioxidant activity, emulsifying activity index, and emulsifying stability index all increased to 73.93%, 15.07 μmol/g, 71.00 or 41.91%, 9.81 m(2)/g, and 67.71%, respectively. Moreover, high-density small and low-flocculation droplets were formed. Therefore, the combined ultrasound treatment and addition of HF to SPI is a more effective method for protein modification compared to ultrasound treatment alone. It provides a theoretical basis for protein processing and application in the future. |
format | Online Article Text |
id | pubmed-8892216 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-88922162022-03-04 Formation of soybean protein isolate-hawthorn flavonoids non-covalent complexes: Linking the physicochemical properties and emulsifying properties Wang, Yi-Lun Yang, Jin-Jie Dai, Shi-Cheng Tong, Xiao-Hong Tian, Tian Liang, Chu-Chen Li, Liang Wang, Huan Jiang, Lian-Zhou Ultrason Sonochem Short Communication In recent years, more and more attention had been paid to the combination of proteins and flavonoids, and several flavonoids had been reported to improve the physicochemical and emulsifying properties of proteins. This study investigated the effects of ultrasonic treatment (450 W for 10 min, 20 min, and 30 min) on the physicochemical properties, antioxidant activity, and emulsifying properties of soy protein isolate (SPI) -hawthorn flavonoids (HF) non-covalent complexes. The results showed that the addition of HF to SPI and 20 min of ultrasound could reduce α-helix and random coil, increase β-sheet and β-turn, and enhance fluorescence quenching. In addition, it decreased the particle size, zeta potential, surface hydrophobicity, and turbidity to 88.43 or 95.27 nm, −28.80 mV, 1250.42, and 0.23, respectively. The protein solubility, free sulfhydryl group, antioxidant activity, emulsifying activity index, and emulsifying stability index all increased to 73.93%, 15.07 μmol/g, 71.00 or 41.91%, 9.81 m(2)/g, and 67.71%, respectively. Moreover, high-density small and low-flocculation droplets were formed. Therefore, the combined ultrasound treatment and addition of HF to SPI is a more effective method for protein modification compared to ultrasound treatment alone. It provides a theoretical basis for protein processing and application in the future. Elsevier 2022-02-25 /pmc/articles/PMC8892216/ /pubmed/35245861 http://dx.doi.org/10.1016/j.ultsonch.2022.105961 Text en © 2022 The Authors https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Short Communication Wang, Yi-Lun Yang, Jin-Jie Dai, Shi-Cheng Tong, Xiao-Hong Tian, Tian Liang, Chu-Chen Li, Liang Wang, Huan Jiang, Lian-Zhou Formation of soybean protein isolate-hawthorn flavonoids non-covalent complexes: Linking the physicochemical properties and emulsifying properties |
title | Formation of soybean protein isolate-hawthorn flavonoids non-covalent complexes: Linking the physicochemical properties and emulsifying properties |
title_full | Formation of soybean protein isolate-hawthorn flavonoids non-covalent complexes: Linking the physicochemical properties and emulsifying properties |
title_fullStr | Formation of soybean protein isolate-hawthorn flavonoids non-covalent complexes: Linking the physicochemical properties and emulsifying properties |
title_full_unstemmed | Formation of soybean protein isolate-hawthorn flavonoids non-covalent complexes: Linking the physicochemical properties and emulsifying properties |
title_short | Formation of soybean protein isolate-hawthorn flavonoids non-covalent complexes: Linking the physicochemical properties and emulsifying properties |
title_sort | formation of soybean protein isolate-hawthorn flavonoids non-covalent complexes: linking the physicochemical properties and emulsifying properties |
topic | Short Communication |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8892216/ https://www.ncbi.nlm.nih.gov/pubmed/35245861 http://dx.doi.org/10.1016/j.ultsonch.2022.105961 |
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