4.7 Article

Recent advance in high-intensity ultrasound modification of blue food protein: Mechanisms, functional properties and structural alterations

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TRENDS IN FOOD SCIENCE & TECHNOLOGY
卷 143, 期 -, 页码 -

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ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tifs.2023.104271

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Blue food proteins; High-intensity ultrasound; Mechanism; Functional properties; Structure

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This review provides a new perspective on the state-of-the-art research and application of high-intensity ultrasound (HIU) for modifying blue food proteins (BFPs). The effects of HIU treatment on the functional properties and structural composition of BFPs are comprehensively evaluated.
Background: Blue food proteins (BFPs) represent a rich and diverse source of high-quality ingredients with outstanding nutritional values and health-beneficial functions, therefore being increasingly paid attention in the food industry. Nevertheless, the low solubility of BFPs and their sensitivity to ambient conditions during processing limit their application. High-intensity ultrasound (HIU) is a promising and effective tool to enhance the functional properties of BFPs by modifying protein structures through the cavitation effect.Scope and approach: This review aims to provide a new horizon of the state-of-the-art research and application of HIU for modifying BFPs. The latest research advancements on the HIU equipment development and effects of HIU treatment on the functional properties and structural composition of BFPs are comprehensively evaluated. Key findings and conclusion: This review reveals that HIU technology is an effective tool for enhancing the functional properties of BFPs. Various techniques such as spectroscopy and electron microscopy were employed to assess the structural changes of BFPs, which are closely related to their functional properties. HIU treatment also significantly impacts the amino acids, digestibility, and antioxidant activity of BFPs. Therefore, the development of HIU equipment and optimization of processing conditions is highly urgent for improving the functional properties of BFPs.

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