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<p>Cold gel formation is an effective method for transferring heat-sensitive compounds or cells. In this study, the effects of whey protein amyloid fibril (AF) and ultrasonic (US) treatment on cold-set whey protein isolate (WPI) gels induced by transglutaminase (TGase) were investigated. Embedding 1% AF in the WPI composite gel and applying US treatment to WPI (gelling agent) enhanced the elastic modulus (<i>G'</i>) from 192.6 to 3526.3&#xa0;Pa and raised the gel hardness by 2.68 times. From a chemical point of view, the domination of β-sheet elements over the other protein secondary structures was observed for all types of WPI composite gels containing AF. The β-sheet structure of AF led to a more rigid WPI gel network induced by TGase. These results conformed to the maximum water holding capacity (WHC) of the AF-ultrasonicated WPI composite gel. US treatment modified the WPI tertiary structure, resulting in an increase in composite elasticity. Application of US treatment to AF resulted in a reduction in its length, followed by its degradation, ultimately leading to the complete loss of its functionality in enhancing rheological properties. In terms of intermolecular interactions, AF influenced the formation of disulfide bonds and hydrophobic interactions. These results demonstrate that TGase-catalyzed WPI-based fiber-hydrogel composites can be strengthened through the combined use of AF (as filler) and US treatment of the continuous gel matrix, without the need for thermal processing or ion addition.</p> Graphical Abstract <p></p>

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Transglutaminase-Catalyzed Composite Gel of Sonicated Amyloid Fibrils-Whey Protein Isolate: The Role of Amyloid Fibrils and Sonication on Rheological and Intermolecular Perspectives

  • 期刊论文

  • 发表日期：

    2026年3月20日

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  • Hoda Khalesi,
  • Katsuyoshi Nishinari,
  • Rassoul Kadkhodaee,
  • Sanjay Mavinkere Rangappa,
  • Suchart Siengchin,
  • Yapeng Fang

摘要

Cold gel formation is an effective method for transferring heat-sensitive compounds or cells. In this study, the effects of whey protein amyloid fibril (AF) and ultrasonic (US) treatment on cold-set whey protein isolate (WPI) gels induced by transglutaminase (TGase) were investigated. Embedding 1% AF in the WPI composite gel and applying US treatment to WPI (gelling agent) enhanced the elastic modulus (G') from 192.6 to 3526.3 Pa and raised the gel hardness by 2.68 times. From a chemical point of view, the domination of β-sheet elements over the other protein secondary structures was observed for all types of WPI composite gels containing AF. The β-sheet structure of AF led to a more rigid WPI gel network induced by TGase. These results conformed to the maximum water holding capacity (WHC) of the AF-ultrasonicated WPI composite gel. US treatment modified the WPI tertiary structure, resulting in an increase in composite elasticity. Application of US treatment to AF resulted in a reduction in its length, followed by its degradation, ultimately leading to the complete loss of its functionality in enhancing rheological properties. In terms of intermolecular interactions, AF influenced the formation of disulfide bonds and hydrophobic interactions. These results demonstrate that TGase-catalyzed WPI-based fiber-hydrogel composites can be strengthened through the combined use of AF (as filler) and US treatment of the continuous gel matrix, without the need for thermal processing or ion addition.

Graphical Abstract