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Microwave-induced heterogeneity in protein conformation and water mobility interferes with the distribution pattern and migration pathway of sodium ion in myofibrillar protein gel
Abstract
The aim of this study was to investigate the distribution pattern and migration pathway of sodium ion in the myofibrillar protein (MP) gel matrix during microwave heating. The results showed that the content of sodium ions in the outer layer of MP gel increased by 47.85% compared with that in the inner layer. In the inner layer of protein gel, the non-covalent disulfide bonds (mainly ε(γ-Glu)-Lys) increased (P < 0.05), which contributed to the formation of a better rigid structure of the protein. The free water content was significantly higher than that of the inner layer (P < 0.05), which was related to the higher mobility of sodium ions. The results of microstructure analysis showed that the outer layer of the MP gel formed a more porous network than the inner layer. This work is expected to give some insights into the development of promising salt-reduced meat products by microwave heating.
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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).”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as M. Zhang, Wei, et al. 2024
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“Proteins distributed around the water molecules were heated rapidly, while proteins buried inside the aggregates were heated slowly, ultimately leading to uneven heating of protein molecules and a T. Shi et al. rough, porous gel morphology (Zhang et al., 2024).”
Metadata
- Authors
- Zhang, M., Wei, T., Mai, Q., Hayat, K., Hou, Y., Xia, S., Cui, H., & Yu, J.
- Affiliations
- Jiangnan University (CN)
- Midea Group (China) (CN)
- Miami University (US)
- Corresponding author
- Xia, Shuqin
- Venue
- Food Chemistry
- Publisher
- Elsevier BV
- Published
- 2024-12
- Volume
- 460
- Issue
- Pt 1
- Pages
- 140503
- ISSN
- 0308-8146 (ISSN-L)
- OpenAlex
- W4400743800
- Cited by
- 24
- References
- 44
- Citations by year
- 2026: 8 · 2025: 14 · 2024: 2
- FWCI
- 5.98
- 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
- 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
- microwave heating, myofibrillar protein gels, sodium ion distribution, ion migration pathways, protein conformation, water mobility, disulfide bonds, free water content, gel microstructure, porous networks
- MeSH terms
- Animals, Gels, Hot Temperature, Meat Products, Microwaves, Muscle Proteins, Myofibrils, Protein Conformation, Sodium, Swine, Water
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