ArticleFoods (Basel, Switzerland)2026
The Stability and Digestive Characteristics of Soybean Protein Fibril/κ-Carrageenan Composite Gels for Riboflavin Encapsulation.
Article in Foods (Basel, Switzerland), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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
1 citing paper in PubMed.
- Role of Anion Identity in the Assembly and Morphology of Whey Protein Isolate Nanofibril Aggregates.Foods (Basel, Switzerland) · 2026Article
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Authors and funding
8 authors.
Funding
Abstract
To address the environmental sensitivity and low bioavailability of riboflavin, this study constructed a soybean protein isolate fibril (SPF)/κ-carrageenan (κC) composite gel delivery system. This study systematically investigated the effects of two independent variables (protein type: SPI/SPF; κC concentration: 2, 4, 6, 8 mg/mL) on the gel structural stability, riboflavin encapsulation performance, and in vitro digestive delivery characteristics of the system. Thioflavin T (ThT) fluorescence and ultraviolet (UV) absorption spectroscopy confirmed the successful preparation of SPF and verified specific intermolecular interactions between SPF and κC. Intermolecular forces, protein leaching rates, and differential scanning calorimetry (DSC) results indicated that compared with SPI-κC composite gels, κC regulates SPF molecular conformation via hydrogen bonding and hydrophobic interactions to exert a synergistic effect. This conformational regulation significantly reduced the protein leaching rates in SPF-κC composite gels, elevated the thermal denaturation temperatures (up to 79.82 °C), and enhanced the gel structural stability. As the κC concentration increased, the environmental stability of SPF-κC riboflavin-loaded composite gels were markedly enhanced, which effectively delayed the gel degradation during simulated gastrointestinal digestion. This was manifested as a reduced protein loss rate (reduced to 22.23%). At a κC concentration of 8 mg/mL, the in vitro release mechanism of riboflavin shifted from Fickian to non-Fickian diffusion.
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Registered trials
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