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Characterization of inhomogeneous Na+ distribution in myofibrillar protein-based emulsion gels during microwave heating and mechanistic insights into migration attenuation
Abstract
This study compared Na+ distribution patterns in protein-based versus emulsified meat products, with a focus on elucidating its migration mechanism in the emulsified systems. The results showed that Na+ content in the outer annulus of emulsion gel demonstrated a 2.23 % to 22.09 % increase compared with the central annulus across varying microwave power. However, emulsion gel exhibited less uneven Na+ distribution compared with protein gels. The conversion of immobile water to free water in outer annulus of emulsion gel was decreased, which was related to the weaken of Na+ mobility. It is noteworthy that the disulfide bonding and hydrophobicity of the protein gels was significantly higher than emulsion gel (P < 0.05), while there were more α-helix and fewer β-sheet in the emulsion gel, which was related to less porous structures and high Na+ mobility in emulsion gel. This study provided a foundation for achieving saltiness control by modulating muscle food microstructure.
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Microwave treatment enables rapid, uniform heating to accelerate denaturation and aggregation of proteins and molecular folding/unfolding that facilitate formation of homogeneous gel networks.
“Microwave treatment enables rapid, uniform heating to accelerate the denaturation and aggregation of proteins and the molecular folding/unfolding that facilitate the formation of homogeneous gel networks (M. Zhang, Wei, et al. 2024; M. Zhang et al. 2025).”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as M. Zhang et al. 2025
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“Microwave treatment enables rapid, uniform heating to accelerate the denaturation and aggregation of proteins and the molecular folding/unfolding that facilitate the formation of homogeneous gel networks (M. Zhang, Wei, et al. 2024 ; M. Zhang et al. 2025 ).”
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Metadata
- Authors
- Zhang, M., Hou, Y., Xia, S., Hayat, K., Cui, H., Yu, J., & Hussain, S.
- Affiliations
- Jiangnan University (CN)
- Parkland College (US)
- King Saud University (SA)
- Corresponding author
- Xia, Shuqin
- Venue
- Food Chemistry
- Publisher
- Elsevier BV
- Published
- 2025-12
- Volume
- 494
- Pages
- 146261
- ISSN
- 0308-8146 (ISSN-L)
- OpenAlex
- W4414040962
- Cited by
- 6
- References
- 36
- Citations by year
- 2026: 2 · 2025: 4
- FWCI
- 3.72
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Food Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Collaborative Innovationcenter of Food Safety and Quality Control in Jiangsu Province (ORF-2025-1073)
- King Saud University
- National Natural Science Foundation of China (32272244)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Meat and Animal Product Quality
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Physical Sciences › Chemistry › Organic Chemistry › Microwave-Assisted Synthesis and Applications
- Keywords
- sodium ion distribution, myofibrillar proteins, emulgel, microwave heating, ion migration
- MeSH terms
- Animals, Cooking, Emulsions, Gels, Hot Temperature, Meat Products, Microwaves, Muscle Proteins, Myofibrils, Sodium, Hydrophobic and Hydrophilic Interactions
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