ArticleFood chemistry: X2023
Effects of ultrasound-assisted high temperature-pressure treatment on the structure and allergenicity of tropomyosin from clam (
Article in Food chemistry: X, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
8 citing papers in PubMed.
- Effect of Boiling onFoods (Basel, Switzerland) · 2025Article
- Reduction in Soybean Flour Allergenicity Through Ball Milling Combined with γ-Aminobutyric Acid Treatment.Foods (Basel, Switzerland) · 2025Article
- Traditional and Emerging Physical Processing Technologies: Applications and Challenges in Allergen Control of Animal and Plant Proteins.Comprehensive reviews in food science and food safety · 2025Review
- Ultrasound and Heat Treatment and Its Potential to Reduce Fennel Allergenicity.Foods (Basel, Switzerland) · 2025Article
- Comprehensive review on the potential of ultrasound for blue food protein extraction, modification and impact on bioactive properties.Ultrasonics sonochemistry · 2024Review
- Recent advances in sustainable marine food utilization: Enhancing chemical, functional, and nutritional properties.Food chemistry: X · 2024Article
- Effect of High-Pressure Processing Treatment on the Physicochemical Properties and Volatile Flavor ofMolecules (Basel, Switzerland) · 2024Article
- Genomics of Shrimp Allergens and Beyond.Genes · 2023Review
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tropomyosin (TM) is the major allergen in clams. This study aimed to evaluate the effects of ultrasound-assisted high temperature-pressure treatment on the structure and allergenicity of TM from clams. The results showed that the combined treatment significantly affected the structure of TM-converting the α-helix to β-sheet and random coil, and decreasing the sulfhydryl group content, surface hydrophobicity, and particle size. These structural changes caused the unfolding of the protein, disrupting and modifying the allergenic epitopes. The significant reduction in the allergenicity of TM was approximately 68.1% when treated with combined processing (
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Registered trials
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