ArticleFoods (Basel, Switzerland)2025
Effect of Transglutaminase-Mediated Cross-Linking on Physicochemical Properties and Structural Modifications of Rice Dreg Protein.
Article in Foods (Basel, Switzerland), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The study examined how transglutaminase (TG)-induced cross-linking affects the structural, functional, and in vitro digestibility characteristics of rice dreg protein (RDP). Analysis using SDS-PAGE showed that low-molecular-weight fragments vanished, while high-molecular-weight polymers formed. Additionally, Fourier transform infrared (FTIR) spectroscopy demonstrated a reduction in β-sheet content alongside an elevation in β-turn structures as the cross-linking process became more pronounced, which was associated with a reduction in both total and free sulfhydryl groups. The hydrophobic nature of the surface and the emulsifying properties of cross-linked RDP initially rose but began to decrease when TG concentrations surpassed 10 U/g of protein. Conversely, emulsion stability and water-binding capacity decreased, while oil-binding capacity improved compared to native RDP. Solubility and in vitro digestibility decreased with cross-linking, whereas rheological properties significantly improved with higher TG levels. These findings suggest that controlled TG-mediated cross-linking (e.g., 10 U/g) effectively enhances the functional properties of RDP, making it a promising ingredient for applications in plant-based meats, baked goods, and fortified beverages within the food industry.
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