Effects of dietary fiber from different particle sizes of wheat bran on myofibrillar protein structure
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Updated: May 6, 2026

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
Published on: September 12, 2019
Jinling Li1, Shunfan Gu1, Ying Mao1
1Department of Food Science and Engineering, Wuhan Polytechnic University, Wuhan 430023, Hubei, China; Hubei Key Laboratory for Processing and Transformation of Agricultural Products (Wuhan Polytechnic University), Wuhan 430023, Hubei, China.
Abstract:
In this study, the effects of wheat bran dietary fiber (WBDF) particle size on the physicochemical properties and structural conformation of myofibrillar protein (MP) were investigated. The results showed that ultrafine comminution effectively reduced the particle size of WBDF from 138.00 μm to 17.53 μm, maintaining a high extraction purity of 90%. Compositional analysis revealed D-xylose and L-arabinose as the dominant monosaccharides (>91%). While the intrinsic hydration capacities of isolated WBDF decreased with smaller particle sizes, the incorporation of micronized WBDF significantly enhanced both the water-holding capacity and oil-holding capacity of the MP composite system. Furthermore, the micronized WBDF significantly stabilized the MP through a novel "hydrophilic shielding" mechanism. Notably, the addition of finer WBDF increased turbidity from 0.20 to 0.47 but reduced surface hydrophobicity (H0) from 1239.10 to 875.90, decreasing by 29.3%. This reduction, coupled with intrinsic fluorescence quenching and a red shift in maximum emission, indicates the formation of a hydration shell around MP molecules by the arabinoxylan-rich fibers, effectively masking hydrophobic domains rather than exposing them. Furthermore, micronized WBDF facilitated the transformation of MP secondary structures toward a more ordered state, characterized by increased α-helix content and enhanced thermal stability. These findings reveal that micronized WBDF can function as a filler and a functional stabilizing agent, enhancing protein structural stability through hydrophilic modification and offering a sustainable strategy for valorizing wheat by-products in meat gel systems.
Insights
Micronized wheat bran dietary fiber (WBDF) improves meat protein stability and water-binding properties. This study shows finer WBDF enhances myofibrillar protein (MP) structure and function, offering a sustainable approach for food applications.
Area of Science:
- Food Science and Technology
- Biochemistry
- Materials Science
Background:
- Wheat bran dietary fiber (WBDF) is a significant agricultural by-product.
- Understanding the impact of WBDF particle size on protein functionality is crucial for food ingredient development.
- Myofibrillar proteins (MP) are key components in meat products, influencing texture and stability.
Purpose of the Study:
- To investigate how different particle sizes of wheat bran dietary fiber (WBDF) affect the physicochemical properties and structural conformation of myofibrillar protein (MP).
- To explore the potential of micronized WBDF as a functional ingredient in protein systems.
- To elucidate the mechanism by which WBDF influences MP stability.
Main Methods:
- Ultrafine comminution of WBDF to reduce particle size.
- Analysis of WBDF composition (monosaccharides).
- Measurement of water-holding capacity (WHC) and oil-holding capacity (OHC) of MP composite systems.
- Assessment of MP surface hydrophobicity and intrinsic fluorescence.
- Analysis of MP secondary structure (e.g., α-helix content) and thermal stability.
Main Results:
- Micronized WBDF (17.53 μm) significantly improved the water-holding and oil-holding capacities of MP.
- WBDF addition reduced MP surface hydrophobicity and induced structural changes, indicating hydrophilic shielding.
- Finer WBDF promoted a more ordered MP secondary structure, increasing α-helix content and thermal stability.
- Arabinoxylan-rich fibers formed a hydration shell around MP, masking hydrophobic domains.
Conclusions:
- Micronized WBDF acts as an effective filler and stabilizer for myofibrillar proteins.
- The "hydrophilic shielding" mechanism enhances protein stability and functional properties.
- This research provides a sustainable strategy for utilizing wheat by-products in meat gel systems and other food applications.
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