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Updated: Jan 29, 2026

Spatial Separation of Molecular Conformers and Clusters
Published on: January 9, 2014
The effects of insoluble dietary fiber on myofibrillar protein gelation: Microstructure and molecular conformations
Xinbo Zhuang1, Minyi Han1, Xiping Jiang2
1MOE Joint International Research Laboratory of Animal Health and Food Safety, Key Lab of Meat Processing and Quality Control, MOE, Jiangsu Collaborative Innovation Center of Meat Production and Processing, Quality and Safety Control, Key Laboratory of Meat Products Processing, MOA, Nanjing Agricultural University, Nanjing 210095, China.
Abstract:
The effects of insoluble dietary fiber (IDF) on heat-induced gelation properties, such as microstructural changes and the molecular conformation of myofibrillar proteins (MP), were analyzed by image analyses and Raman spectroscopy. Scanning electron microscopy revealed that pure MP gelation contained a loose and dispersed network with interconnected water channels. With IDF addition, the lacunarity and the particle size of water pores both significantly decreased (P < 0.05) and fractal dimension significantly increased (P < 0.05), which indicated the formation of a homogenous and compact three-dimensional network. Through Raman spectra, IDF addition resulted in modification of amide I and III regions, by a significant decrease in α-helix content, accompanied by an increase of β-sheets, β-turns, and random coil content (P < 0.05); the intensity of CU+005CH stretching vibrations bending vibrations bands were significantly decreased (P < 0.05). Principal component analyses showed significant correlations between textual property, microstructure and molecular conformations. Cluster analyses indicated IDF improved the functionality of MP gel by 1): IDF stable the moisture phase 2) "concentrated" MP promoted structural integrity and compact gelation.
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