ArticleMolecules (Basel, Switzerland)2025
Does Transglutaminase Crosslinking Reduce the Antibody Recognition Capacity of β-Lactoglobulin: An Analysis from Conformational Perspective.
Article in Molecules (Basel, Switzerland), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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.
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Who cites it
2 citing papers in PubMed.
- Bibliometric Analysis of Cow's Milk Protein Allergy Research in the Past Two Decades.Journal of inflammation research · 2026Article
- Advances in Food Processing Techniques for Allergenicity Reduction and Allergen Identification.Foods (Basel, Switzerland) · 2025Review
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Authors and funding
9 authors.
Funding
Abstract
Food allergies are a global concern, with β-lactoglobulin (β-LG) in bovine milk being a major allergenic protein. This study investigated the effects of transglutaminase (TGase)-mediated crosslinking on the antibody recognition capacity (ARC) and structural properties of β-LG, with the aim of developing hypoallergenic dairy products. β-LG solutions were treated with TGase at varying concentrations (0, 5, 10, 15, and 20 U/g) and durations (0, 6, 18, 24, and 42 h), followed by analysis using electrophoresis, enzyme-linked immunosorbent assay (ELISA), and spectroscopy. The results demonstrated that treatment with TGase at 20 U/g significantly reduced the ARC and immunoglobulin E (IgE) binding capacity of β-LG to 90.0 ± 0.4% and 58.4 ± 1.0%, respectively, with the optimal ARC reduction observed after 6 h of treatment (86.7 ± 1.2%,
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Registered trials
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