Effect of Ionic Strength on Heat-Induced Gelation Behavior of Soy Protein Isolates with Ultrasound Treatment

This study investigated the effect of ultrasound on gel properties of soy protein isolates (SPIs) at different salt concentrations. The results showed that ultrasound could significantly improve the gel hardness and the water holding capacity (WHC) of the salt-containing gel (<i<p</i< &l...
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Autor*in:	Zhaojun Wang [verfasserIn] Lin Zeng [verfasserIn] Liwei Fu [verfasserIn] Qiuming Chen [verfasserIn] Zhiyong He [verfasserIn] Maomao Zeng [verfasserIn] Fang Qin [verfasserIn] Jie Chen [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2022

Schlagwörter:	soy protein isolates gel properties NaCl concentration ultrasound rheological properties protein interaction

Übergeordnetes Werk:	In: Molecules - MDPI AG, 2003, 27(2022), 23, p 8221
Übergeordnetes Werk:	volume:27 ; year:2022 ; number:23, p 8221

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/molecules27238221

Katalog-ID:	DOAJ083416005

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520			\|a This study investigated the effect of ultrasound on gel properties of soy protein isolates (SPIs) at different salt concentrations. The results showed that ultrasound could significantly improve the gel hardness and the water holding capacity (WHC) of the salt-containing gel (<i<p</i< < 0.05). The gel presents a uniform and compact three-dimensional network structure. The combination of 200 mM NaCl with 20 min of ultrasound could significantly increase the gel hardness (four times) and the WHC (<i<p</i< < 0.05) compared with the SPI gel without treatment. With the increase in NaCl concentration, the ζ potential and surface hydrophobicity increased, and the solubility decreased. Ultrasound could improve the protein solubility, compensate for the loss of solubility caused by the addition of NaCl, and further increase the surface hydrophobicity. Ultrasound combined with NaCl allowed proteins to form aggregates of different sizes. In addition, the combined treatment increased the hydrophobic interactions and disulfide bond interactions in the gel. Overall, ultrasound could improve the thermal gel properties of SPI gels with salt addition.
650		4	\|a soy protein isolates
650		4	\|a gel properties
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650		4	\|a ultrasound
650		4	\|a rheological properties
650		4	\|a protein interaction
653		0	\|a Organic chemistry
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allfields	10.3390/molecules27238221 doi (DE-627)DOAJ083416005 (DE-599)DOAJ31fc2b2a77074d53ae1968ae462d332a DE-627 ger DE-627 rakwb eng QD241-441 Zhaojun Wang verfasserin aut Effect of Ionic Strength on Heat-Induced Gelation Behavior of Soy Protein Isolates with Ultrasound Treatment 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier This study investigated the effect of ultrasound on gel properties of soy protein isolates (SPIs) at different salt concentrations. The results showed that ultrasound could significantly improve the gel hardness and the water holding capacity (WHC) of the salt-containing gel (<i<p</i< < 0.05). The gel presents a uniform and compact three-dimensional network structure. The combination of 200 mM NaCl with 20 min of ultrasound could significantly increase the gel hardness (four times) and the WHC (<i<p</i< < 0.05) compared with the SPI gel without treatment. With the increase in NaCl concentration, the ζ potential and surface hydrophobicity increased, and the solubility decreased. Ultrasound could improve the protein solubility, compensate for the loss of solubility caused by the addition of NaCl, and further increase the surface hydrophobicity. Ultrasound combined with NaCl allowed proteins to form aggregates of different sizes. In addition, the combined treatment increased the hydrophobic interactions and disulfide bond interactions in the gel. Overall, ultrasound could improve the thermal gel properties of SPI gels with salt addition. soy protein isolates gel properties NaCl concentration ultrasound rheological properties protein interaction Organic chemistry Lin Zeng verfasserin aut Liwei Fu verfasserin aut Qiuming Chen verfasserin aut Zhiyong He verfasserin aut Maomao Zeng verfasserin aut Fang Qin verfasserin aut Jie Chen verfasserin aut In Molecules MDPI AG, 2003 27(2022), 23, p 8221 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:27 year:2022 number:23, p 8221 https://doi.org/10.3390/molecules27238221 kostenfrei https://doaj.org/article/31fc2b2a77074d53ae1968ae462d332a kostenfrei https://www.mdpi.com/1420-3049/27/23/8221 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 27 2022 23, p 8221
spelling	10.3390/molecules27238221 doi (DE-627)DOAJ083416005 (DE-599)DOAJ31fc2b2a77074d53ae1968ae462d332a DE-627 ger DE-627 rakwb eng QD241-441 Zhaojun Wang verfasserin aut Effect of Ionic Strength on Heat-Induced Gelation Behavior of Soy Protein Isolates with Ultrasound Treatment 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier This study investigated the effect of ultrasound on gel properties of soy protein isolates (SPIs) at different salt concentrations. The results showed that ultrasound could significantly improve the gel hardness and the water holding capacity (WHC) of the salt-containing gel (<i<p</i< < 0.05). The gel presents a uniform and compact three-dimensional network structure. The combination of 200 mM NaCl with 20 min of ultrasound could significantly increase the gel hardness (four times) and the WHC (<i<p</i< < 0.05) compared with the SPI gel without treatment. With the increase in NaCl concentration, the ζ potential and surface hydrophobicity increased, and the solubility decreased. Ultrasound could improve the protein solubility, compensate for the loss of solubility caused by the addition of NaCl, and further increase the surface hydrophobicity. Ultrasound combined with NaCl allowed proteins to form aggregates of different sizes. In addition, the combined treatment increased the hydrophobic interactions and disulfide bond interactions in the gel. Overall, ultrasound could improve the thermal gel properties of SPI gels with salt addition. soy protein isolates gel properties NaCl concentration ultrasound rheological properties protein interaction Organic chemistry Lin Zeng verfasserin aut Liwei Fu verfasserin aut Qiuming Chen verfasserin aut Zhiyong He verfasserin aut Maomao Zeng verfasserin aut Fang Qin verfasserin aut Jie Chen verfasserin aut In Molecules MDPI AG, 2003 27(2022), 23, p 8221 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:27 year:2022 number:23, p 8221 https://doi.org/10.3390/molecules27238221 kostenfrei https://doaj.org/article/31fc2b2a77074d53ae1968ae462d332a kostenfrei https://www.mdpi.com/1420-3049/27/23/8221 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 27 2022 23, p 8221
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allfieldsGer	10.3390/molecules27238221 doi (DE-627)DOAJ083416005 (DE-599)DOAJ31fc2b2a77074d53ae1968ae462d332a DE-627 ger DE-627 rakwb eng QD241-441 Zhaojun Wang verfasserin aut Effect of Ionic Strength on Heat-Induced Gelation Behavior of Soy Protein Isolates with Ultrasound Treatment 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier This study investigated the effect of ultrasound on gel properties of soy protein isolates (SPIs) at different salt concentrations. The results showed that ultrasound could significantly improve the gel hardness and the water holding capacity (WHC) of the salt-containing gel (<i<p</i< < 0.05). The gel presents a uniform and compact three-dimensional network structure. The combination of 200 mM NaCl with 20 min of ultrasound could significantly increase the gel hardness (four times) and the WHC (<i<p</i< < 0.05) compared with the SPI gel without treatment. With the increase in NaCl concentration, the ζ potential and surface hydrophobicity increased, and the solubility decreased. Ultrasound could improve the protein solubility, compensate for the loss of solubility caused by the addition of NaCl, and further increase the surface hydrophobicity. Ultrasound combined with NaCl allowed proteins to form aggregates of different sizes. In addition, the combined treatment increased the hydrophobic interactions and disulfide bond interactions in the gel. Overall, ultrasound could improve the thermal gel properties of SPI gels with salt addition. soy protein isolates gel properties NaCl concentration ultrasound rheological properties protein interaction Organic chemistry Lin Zeng verfasserin aut Liwei Fu verfasserin aut Qiuming Chen verfasserin aut Zhiyong He verfasserin aut Maomao Zeng verfasserin aut Fang Qin verfasserin aut Jie Chen verfasserin aut In Molecules MDPI AG, 2003 27(2022), 23, p 8221 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:27 year:2022 number:23, p 8221 https://doi.org/10.3390/molecules27238221 kostenfrei https://doaj.org/article/31fc2b2a77074d53ae1968ae462d332a kostenfrei https://www.mdpi.com/1420-3049/27/23/8221 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 27 2022 23, p 8221
allfieldsSound	10.3390/molecules27238221 doi (DE-627)DOAJ083416005 (DE-599)DOAJ31fc2b2a77074d53ae1968ae462d332a DE-627 ger DE-627 rakwb eng QD241-441 Zhaojun Wang verfasserin aut Effect of Ionic Strength on Heat-Induced Gelation Behavior of Soy Protein Isolates with Ultrasound Treatment 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier This study investigated the effect of ultrasound on gel properties of soy protein isolates (SPIs) at different salt concentrations. The results showed that ultrasound could significantly improve the gel hardness and the water holding capacity (WHC) of the salt-containing gel (<i<p</i< < 0.05). The gel presents a uniform and compact three-dimensional network structure. The combination of 200 mM NaCl with 20 min of ultrasound could significantly increase the gel hardness (four times) and the WHC (<i<p</i< < 0.05) compared with the SPI gel without treatment. With the increase in NaCl concentration, the ζ potential and surface hydrophobicity increased, and the solubility decreased. Ultrasound could improve the protein solubility, compensate for the loss of solubility caused by the addition of NaCl, and further increase the surface hydrophobicity. Ultrasound combined with NaCl allowed proteins to form aggregates of different sizes. In addition, the combined treatment increased the hydrophobic interactions and disulfide bond interactions in the gel. Overall, ultrasound could improve the thermal gel properties of SPI gels with salt addition. soy protein isolates gel properties NaCl concentration ultrasound rheological properties protein interaction Organic chemistry Lin Zeng verfasserin aut Liwei Fu verfasserin aut Qiuming Chen verfasserin aut Zhiyong He verfasserin aut Maomao Zeng verfasserin aut Fang Qin verfasserin aut Jie Chen verfasserin aut In Molecules MDPI AG, 2003 27(2022), 23, p 8221 (DE-627)311313132 (DE-600)2008644-1 14203049 nnns volume:27 year:2022 number:23, p 8221 https://doi.org/10.3390/molecules27238221 kostenfrei https://doaj.org/article/31fc2b2a77074d53ae1968ae462d332a kostenfrei https://www.mdpi.com/1420-3049/27/23/8221 kostenfrei https://doaj.org/toc/1420-3049 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 27 2022 23, p 8221
language	English
source	In Molecules 27(2022), 23, p 8221 volume:27 year:2022 number:23, p 8221
sourceStr	In Molecules 27(2022), 23, p 8221 volume:27 year:2022 number:23, p 8221
format_phy_str_mv	Article
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topic_facet	soy protein isolates gel properties NaCl concentration ultrasound rheological properties protein interaction Organic chemistry
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container_title	Molecules
authorswithroles_txt_mv	Zhaojun Wang @@aut@@ Lin Zeng @@aut@@ Liwei Fu @@aut@@ Qiuming Chen @@aut@@ Zhiyong He @@aut@@ Maomao Zeng @@aut@@ Fang Qin @@aut@@ Jie Chen @@aut@@
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callnumber-first	Q - Science
author	Zhaojun Wang
spellingShingle	Zhaojun Wang misc QD241-441 misc soy protein isolates misc gel properties misc NaCl concentration misc ultrasound misc rheological properties misc protein interaction misc Organic chemistry Effect of Ionic Strength on Heat-Induced Gelation Behavior of Soy Protein Isolates with Ultrasound Treatment
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topic_title	QD241-441 Effect of Ionic Strength on Heat-Induced Gelation Behavior of Soy Protein Isolates with Ultrasound Treatment soy protein isolates gel properties NaCl concentration ultrasound rheological properties protein interaction
topic	misc QD241-441 misc soy protein isolates misc gel properties misc NaCl concentration misc ultrasound misc rheological properties misc protein interaction misc Organic chemistry
topic_unstemmed	misc QD241-441 misc soy protein isolates misc gel properties misc NaCl concentration misc ultrasound misc rheological properties misc protein interaction misc Organic chemistry
topic_browse	misc QD241-441 misc soy protein isolates misc gel properties misc NaCl concentration misc ultrasound misc rheological properties misc protein interaction misc Organic chemistry
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title	Effect of Ionic Strength on Heat-Induced Gelation Behavior of Soy Protein Isolates with Ultrasound Treatment
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title_full	Effect of Ionic Strength on Heat-Induced Gelation Behavior of Soy Protein Isolates with Ultrasound Treatment
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author_browse	Zhaojun Wang Lin Zeng Liwei Fu Qiuming Chen Zhiyong He Maomao Zeng Fang Qin Jie Chen
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title_sort	effect of ionic strength on heat-induced gelation behavior of soy protein isolates with ultrasound treatment
callnumber	QD241-441
title_auth	Effect of Ionic Strength on Heat-Induced Gelation Behavior of Soy Protein Isolates with Ultrasound Treatment
abstract	This study investigated the effect of ultrasound on gel properties of soy protein isolates (SPIs) at different salt concentrations. The results showed that ultrasound could significantly improve the gel hardness and the water holding capacity (WHC) of the salt-containing gel (<i<p</i< < 0.05). The gel presents a uniform and compact three-dimensional network structure. The combination of 200 mM NaCl with 20 min of ultrasound could significantly increase the gel hardness (four times) and the WHC (<i<p</i< < 0.05) compared with the SPI gel without treatment. With the increase in NaCl concentration, the ζ potential and surface hydrophobicity increased, and the solubility decreased. Ultrasound could improve the protein solubility, compensate for the loss of solubility caused by the addition of NaCl, and further increase the surface hydrophobicity. Ultrasound combined with NaCl allowed proteins to form aggregates of different sizes. In addition, the combined treatment increased the hydrophobic interactions and disulfide bond interactions in the gel. Overall, ultrasound could improve the thermal gel properties of SPI gels with salt addition.
abstractGer	This study investigated the effect of ultrasound on gel properties of soy protein isolates (SPIs) at different salt concentrations. The results showed that ultrasound could significantly improve the gel hardness and the water holding capacity (WHC) of the salt-containing gel (<i<p</i< < 0.05). The gel presents a uniform and compact three-dimensional network structure. The combination of 200 mM NaCl with 20 min of ultrasound could significantly increase the gel hardness (four times) and the WHC (<i<p</i< < 0.05) compared with the SPI gel without treatment. With the increase in NaCl concentration, the ζ potential and surface hydrophobicity increased, and the solubility decreased. Ultrasound could improve the protein solubility, compensate for the loss of solubility caused by the addition of NaCl, and further increase the surface hydrophobicity. Ultrasound combined with NaCl allowed proteins to form aggregates of different sizes. In addition, the combined treatment increased the hydrophobic interactions and disulfide bond interactions in the gel. Overall, ultrasound could improve the thermal gel properties of SPI gels with salt addition.
abstract_unstemmed	This study investigated the effect of ultrasound on gel properties of soy protein isolates (SPIs) at different salt concentrations. The results showed that ultrasound could significantly improve the gel hardness and the water holding capacity (WHC) of the salt-containing gel (<i<p</i< < 0.05). The gel presents a uniform and compact three-dimensional network structure. The combination of 200 mM NaCl with 20 min of ultrasound could significantly increase the gel hardness (four times) and the WHC (<i<p</i< < 0.05) compared with the SPI gel without treatment. With the increase in NaCl concentration, the ζ potential and surface hydrophobicity increased, and the solubility decreased. Ultrasound could improve the protein solubility, compensate for the loss of solubility caused by the addition of NaCl, and further increase the surface hydrophobicity. Ultrasound combined with NaCl allowed proteins to form aggregates of different sizes. In addition, the combined treatment increased the hydrophobic interactions and disulfide bond interactions in the gel. Overall, ultrasound could improve the thermal gel properties of SPI gels with salt addition.
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container_issue	23, p 8221
title_short	Effect of Ionic Strength on Heat-Induced Gelation Behavior of Soy Protein Isolates with Ultrasound Treatment
url	https://doi.org/10.3390/molecules27238221 https://doaj.org/article/31fc2b2a77074d53ae1968ae462d332a https://www.mdpi.com/1420-3049/27/23/8221 https://doaj.org/toc/1420-3049
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Effect of Ionic Strength on Heat-Induced Gelation Behavior of Soy Protein Isolates with Ultrasound Treatment

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