<p>Plant-based proteins are considered an alternative to animal-based proteins due to their potentially lower impact on human nutrition. Ultrasound techniques have been employed in food applications to modify plant-based proteins primarily through chemical and physical property, thereby enhancing food quality. This review elucidates the technology, mechanisms, applications, and functional properties of plant-based proteins. Sonication induces structural modifications through cavitation, generating intense shear forces that disrupt hydrogen bonds, alter hydrophobic interactions, and facilitate partial unfolding of protein molecules. These modifications affect all levels of protein structure (primary, secondary, tertiary, and quaternary), resulting in more flexible and less compact conformations. These structural transitions improve protein digestibility and enhance key functional properties, including solubility, emulsification, gelation, and foaming behavior. In summary, ultrasound technology represents a promising non-thermal approach for tailoring plant-based protein functionality, thereby supporting the development of high-quality, sustainable food products.</p>

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Ultrasound technique: structure-function relationship of plant-based proteins and digestibility in food applications

  • Mohammad Alrosan,
  • Sofyan Maghaydah,
  • Taher Assaf,
  • Hadeel J. Obeidat,
  • Hiba Bawadi,
  • Muhammad H. Alu’datt,
  • Ali Madi Almajwal,
  • Aya Alqasrawi,
  • Nrdeen Alhaleeq,
  • Saif Elmoumani,
  • Thuan-Chew Tan

摘要

Plant-based proteins are considered an alternative to animal-based proteins due to their potentially lower impact on human nutrition. Ultrasound techniques have been employed in food applications to modify plant-based proteins primarily through chemical and physical property, thereby enhancing food quality. This review elucidates the technology, mechanisms, applications, and functional properties of plant-based proteins. Sonication induces structural modifications through cavitation, generating intense shear forces that disrupt hydrogen bonds, alter hydrophobic interactions, and facilitate partial unfolding of protein molecules. These modifications affect all levels of protein structure (primary, secondary, tertiary, and quaternary), resulting in more flexible and less compact conformations. These structural transitions improve protein digestibility and enhance key functional properties, including solubility, emulsification, gelation, and foaming behavior. In summary, ultrasound technology represents a promising non-thermal approach for tailoring plant-based protein functionality, thereby supporting the development of high-quality, sustainable food products.