Effect of high intensity ultrasound on the structure and solubility of soy protein isolate-pectin complex

In this study, a soy protein isolate (SPI)-pectin (PC) complex was prepared, and the effects of different high intensity ultrasound (HIU) powers on the structure and solubility of the complex were studied. Fourier transform infrared (FTIR) spectroscopy analysis exhibited that with increasing HIU pow...

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Autores principales:	Ning Wang, Xiaonan Zhou, Weining Wang, Liqi Wang, Lianzhou Jiang, Tianyi Liu, Dianyu Yu
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	High intensity ultrasound Soy protein isolate Pectin Structural properties Solubility Chemistry QD1-999 Acoustics. Sound QC221-246
Acceso en línea:	https://doaj.org/article/0e680d2bdf424ad09cfe18acd9f94a03
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spelling	oai:doaj.org-article:0e680d2bdf424ad09cfe18acd9f94a032021-12-02T04:59:47ZEffect of high intensity ultrasound on the structure and solubility of soy protein isolate-pectin complex1350-417710.1016/j.ultsonch.2021.105808https://doaj.org/article/0e680d2bdf424ad09cfe18acd9f94a032021-12-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S1350417721003503https://doaj.org/toc/1350-4177In this study, a soy protein isolate (SPI)-pectin (PC) complex was prepared, and the effects of different high intensity ultrasound (HIU) powers on the structure and solubility of the complex were studied. Fourier transform infrared (FTIR) spectroscopy analysis exhibited that with increasing HIU power, the α-helix content of the SPI in the complex was significantly reduced, and the random coil content increased; however, an opposite trend appeared after higher power treatments. Fluorescence spectra showed that HIU treatment increased the fluorescence intensity of the complex, and the surface hydrophobicity was increased. The trend of the protein structure studied by Raman spectroscopy was similar to that of FTIR and fluorescence spectroscopy. When the HIU treatment was performed for 15 min and at 450 W power, the particle size of the complex was 451.85 ± 2.17 nm, and the solubility was 89.04 ± 0.19 %, indicating that the HIU treatment caused the spatial conformation of the protein to loosen and improved the functional properties of the complex. Confocal laser scanning microscopy (CLSM) revealed that the complex after HIU treatment exhibited improved dispersibility in water and smaller particle size. Gel electrophoresis results indicated that HIU treatment did not affect the protein subunits of the complex. Therefore, the selection of a suitable HIU treatment power can effectively improve the structural properties and solubility of SPI in the complex, and promote the application of the SPI-PC complex in food processing and industries.Ning WangXiaonan ZhouWeining WangLiqi WangLianzhou JiangTianyi LiuDianyu YuElsevierarticleHigh intensity ultrasoundSoy protein isolatePectinStructural propertiesSolubilityChemistryQD1-999Acoustics. SoundQC221-246ENUltrasonics Sonochemistry, Vol 80, Iss , Pp 105808- (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	High intensity ultrasound Soy protein isolate Pectin Structural properties Solubility Chemistry QD1-999 Acoustics. Sound QC221-246
spellingShingle	High intensity ultrasound Soy protein isolate Pectin Structural properties Solubility Chemistry QD1-999 Acoustics. Sound QC221-246 Ning Wang Xiaonan Zhou Weining Wang Liqi Wang Lianzhou Jiang Tianyi Liu Dianyu Yu Effect of high intensity ultrasound on the structure and solubility of soy protein isolate-pectin complex
description	In this study, a soy protein isolate (SPI)-pectin (PC) complex was prepared, and the effects of different high intensity ultrasound (HIU) powers on the structure and solubility of the complex were studied. Fourier transform infrared (FTIR) spectroscopy analysis exhibited that with increasing HIU power, the α-helix content of the SPI in the complex was significantly reduced, and the random coil content increased; however, an opposite trend appeared after higher power treatments. Fluorescence spectra showed that HIU treatment increased the fluorescence intensity of the complex, and the surface hydrophobicity was increased. The trend of the protein structure studied by Raman spectroscopy was similar to that of FTIR and fluorescence spectroscopy. When the HIU treatment was performed for 15 min and at 450 W power, the particle size of the complex was 451.85 ± 2.17 nm, and the solubility was 89.04 ± 0.19 %, indicating that the HIU treatment caused the spatial conformation of the protein to loosen and improved the functional properties of the complex. Confocal laser scanning microscopy (CLSM) revealed that the complex after HIU treatment exhibited improved dispersibility in water and smaller particle size. Gel electrophoresis results indicated that HIU treatment did not affect the protein subunits of the complex. Therefore, the selection of a suitable HIU treatment power can effectively improve the structural properties and solubility of SPI in the complex, and promote the application of the SPI-PC complex in food processing and industries.
format	article
author	Ning Wang Xiaonan Zhou Weining Wang Liqi Wang Lianzhou Jiang Tianyi Liu Dianyu Yu
author_facet	Ning Wang Xiaonan Zhou Weining Wang Liqi Wang Lianzhou Jiang Tianyi Liu Dianyu Yu
author_sort	Ning Wang
title	Effect of high intensity ultrasound on the structure and solubility of soy protein isolate-pectin complex
title_short	Effect of high intensity ultrasound on the structure and solubility of soy protein isolate-pectin complex
title_full	Effect of high intensity ultrasound on the structure and solubility of soy protein isolate-pectin complex
title_fullStr	Effect of high intensity ultrasound on the structure and solubility of soy protein isolate-pectin complex
title_full_unstemmed	Effect of high intensity ultrasound on the structure and solubility of soy protein isolate-pectin complex
title_sort	effect of high intensity ultrasound on the structure and solubility of soy protein isolate-pectin complex
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/0e680d2bdf424ad09cfe18acd9f94a03
work_keys_str_mv	AT ningwang effectofhighintensityultrasoundonthestructureandsolubilityofsoyproteinisolatepectincomplex AT xiaonanzhou effectofhighintensityultrasoundonthestructureandsolubilityofsoyproteinisolatepectincomplex AT weiningwang effectofhighintensityultrasoundonthestructureandsolubilityofsoyproteinisolatepectincomplex AT liqiwang effectofhighintensityultrasoundonthestructureandsolubilityofsoyproteinisolatepectincomplex AT lianzhoujiang effectofhighintensityultrasoundonthestructureandsolubilityofsoyproteinisolatepectincomplex AT tianyiliu effectofhighintensityultrasoundonthestructureandsolubilityofsoyproteinisolatepectincomplex AT dianyuyu effectofhighintensityultrasoundonthestructureandsolubilityofsoyproteinisolatepectincomplex
_version_	1718400873960308736

Effect of high intensity ultrasound on the structure and solubility of soy protein isolate-pectin complex

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