ArticleFood chemistry: X2025
Tuning oxidative stability and digestibility of frozen myofibrillar protein: A combined magnetic field and pH-shifting approach.
Article in Food chemistry: X, 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.
- Impact of Novel and Emerging Nonthermal Technologies on the Functionality and Digestibility of Poultry-Derived Proteins.Foods (Basel, Switzerland) · 2026Review
- Functional and Interfacial Responses of Honeybee Pupa Water-Soluble Proteins to pH, Ionic Strength, and Sucrose.Foods (Basel, Switzerland) · 2026Article
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Authors and funding
7 authors.
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Abstract
This study investigated the synergistic effects of magnetic field (MF) and pH-shifting (pH 9-11) on the oxidative stability and in vitro digestibility of frozen denatured myofibrillar protein (MP). Results revealed that MF-assisted pH-shifting at pH 9 (MP-9 + MF) exhibited the better synergistic effect, significantly enhancing oxidative stability by promoting a compact, ordered protein conformation that minimized carbonyl formation and preserved sulfhydryl content. However, pH-shifting at pH 10 without MF achieved the highest in vitro digestibility, but this benefit came at the cost of reduced oxidative stability, as evidenced by the significant increase in carbonyl content. These findings demonstrate that this combined approach presents a clear trade-off, allowing for the targeted modulation of MP properties to prioritize either oxidative stability or digestibility, providing a novel strategy to enhance the quality of meat products.
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