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Improved Gel Properties of Whey Protein-Stabilized Emulsions by Ultrasound and Enzymatic Cross-Linking

This study investigated the effects of high-intensity ultrasound (HUS) and transglutaminase pretreatment on the gelation behavior of whey protein soluble aggregate (WPISA) emulsions. HUS pretreatment and TGase-mediated cross-linking delayed the onset of gelation but significantly increased (p < 0...

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Autores principales: Zhao, Yanli, Xue, Shiqi, Zhang, Xinyue, Zhang, Tiehua, Shen, Xue
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8482177/
https://www.ncbi.nlm.nih.gov/pubmed/34563021
http://dx.doi.org/10.3390/gels7030135
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author Zhao, Yanli
Xue, Shiqi
Zhang, Xinyue
Zhang, Tiehua
Shen, Xue
author_facet Zhao, Yanli
Xue, Shiqi
Zhang, Xinyue
Zhang, Tiehua
Shen, Xue
author_sort Zhao, Yanli
collection PubMed
description This study investigated the effects of high-intensity ultrasound (HUS) and transglutaminase pretreatment on the gelation behavior of whey protein soluble aggregate (WPISA) emulsions. HUS pretreatment and TGase-mediated cross-linking delayed the onset of gelation but significantly increased (p < 0.05) the gel firmness (G′) both after gel formation at 25 °C and during storage at 4 °C. The frequency sweep test indicated that all gels had a similar frequency dependence at 4 and 25 °C, and the elasticity and viscosity of the WPISA-stabilized emulsion gel were significantly enhanced by HUS pretreatment and TGase-mediated cross-linking (p < 0.05). HUS and TGase-mediated cross-linking greatly improved the textural properties of WPISA-stabilized emulsion gels, as revealed by their increases in gel hardness, cohesiveness, resilience, and chewiness. HUS pretreatment and TGase-mediated cross-linking significantly increased the water-holding capacity but decreased the swelling ratios of the gels (p < 0.05). Interactive force analysis confirmed that noncovalent interactions, disulfide bonds, and TGase-induced covalent cross-links were all involved in the formation of gel networks. In conclusion, the combination of HUS and TGase-mediated cross-linking were beneficial for improving the gelation properties of WPISA-stabilized emulsion as a controlled release vehicle for potential food industrial applications.
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spelling pubmed-84821772021-10-01 Improved Gel Properties of Whey Protein-Stabilized Emulsions by Ultrasound and Enzymatic Cross-Linking Zhao, Yanli Xue, Shiqi Zhang, Xinyue Zhang, Tiehua Shen, Xue Gels Article This study investigated the effects of high-intensity ultrasound (HUS) and transglutaminase pretreatment on the gelation behavior of whey protein soluble aggregate (WPISA) emulsions. HUS pretreatment and TGase-mediated cross-linking delayed the onset of gelation but significantly increased (p < 0.05) the gel firmness (G′) both after gel formation at 25 °C and during storage at 4 °C. The frequency sweep test indicated that all gels had a similar frequency dependence at 4 and 25 °C, and the elasticity and viscosity of the WPISA-stabilized emulsion gel were significantly enhanced by HUS pretreatment and TGase-mediated cross-linking (p < 0.05). HUS and TGase-mediated cross-linking greatly improved the textural properties of WPISA-stabilized emulsion gels, as revealed by their increases in gel hardness, cohesiveness, resilience, and chewiness. HUS pretreatment and TGase-mediated cross-linking significantly increased the water-holding capacity but decreased the swelling ratios of the gels (p < 0.05). Interactive force analysis confirmed that noncovalent interactions, disulfide bonds, and TGase-induced covalent cross-links were all involved in the formation of gel networks. In conclusion, the combination of HUS and TGase-mediated cross-linking were beneficial for improving the gelation properties of WPISA-stabilized emulsion as a controlled release vehicle for potential food industrial applications. MDPI 2021-09-09 /pmc/articles/PMC8482177/ /pubmed/34563021 http://dx.doi.org/10.3390/gels7030135 Text en © 2021 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
Zhao, Yanli
Xue, Shiqi
Zhang, Xinyue
Zhang, Tiehua
Shen, Xue
Improved Gel Properties of Whey Protein-Stabilized Emulsions by Ultrasound and Enzymatic Cross-Linking
title Improved Gel Properties of Whey Protein-Stabilized Emulsions by Ultrasound and Enzymatic Cross-Linking
title_full Improved Gel Properties of Whey Protein-Stabilized Emulsions by Ultrasound and Enzymatic Cross-Linking
title_fullStr Improved Gel Properties of Whey Protein-Stabilized Emulsions by Ultrasound and Enzymatic Cross-Linking
title_full_unstemmed Improved Gel Properties of Whey Protein-Stabilized Emulsions by Ultrasound and Enzymatic Cross-Linking
title_short Improved Gel Properties of Whey Protein-Stabilized Emulsions by Ultrasound and Enzymatic Cross-Linking
title_sort improved gel properties of whey protein-stabilized emulsions by ultrasound and enzymatic cross-linking
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8482177/
https://www.ncbi.nlm.nih.gov/pubmed/34563021
http://dx.doi.org/10.3390/gels7030135
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