Effects of Thermal Denaturation on the Interactions Between Soluble Soybean Polysaccharides and Casein and Whey Protein

This study aimed to investigate the interactions between soluble soybean polysaccharides (SSPS) and milk proteins, namely, casein and whey protein, and to evaluate their effects on the stability of acidified milk beverages under different degrees of thermal denaturation. Casein, whey protein, and SSPS were used as raw materials to prepare mixed solutions under varying pH conditions. A combination of analytical techniques, including centrifugal sedimentation rate, particle size distribution, ζ-potential measurement, differential scanning calorimetry (DSC), size-exclusion chromatography (SEC), and LUMisizer stability analysis, was employed to systematically examine the interactions between SSPS and the two proteins, as well as the influence of thermal treatment at 120-140 °C (casein) and 65-78 °C (whey protein). The results demonstrated that under acidic conditions (pH 3.5-4.5), SSPS formed compact complexes with casein, effectively stabilizing casein dispersions through steric hindrance and electrostatic repulsion. In contrast, SSPS exhibited a limited stabilizing ability toward whey protein due to its strong tendency to aggregate, which hindered the formation of uniform complexes. Regarding thermal denaturation, casein heated at 140 °C for more than 40 min showed pronounced κ-casein dissociation and aggregation, resulting in reduced stability of the SSPS-casein system. For whey protein, increasing thermal denaturation (complete denaturation at 78 °C for 30 min) led to the formation of larger aggregates, with particle size increasing from 198.23 nm to 213.33 nm and ζ-potential decreasing from -3.77 mV to -2.01 mV, thereby diminishing the stability of the SSPS-whey protein system. Overall, this study elucidates the interaction mechanisms of SSPS with casein and whey protein, and highlights the role of thermal denaturation, thereby providing theoretical guidance for the effective application of SSPS in acidified milk beverages.

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Publication Details

Journal
Molecules
Published
2025-10-28
DOI
https://doi.org/10.3390/molecules30214207
Primary Topic
Proteins in Food Systems
Type
article
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article

Effects of Thermal Denaturation on the Interactions Between Soluble Soybean Polysaccharides and Casein and Whey Protein

Hongyang Pan, Shenghu Zhou, Xiaofang Chu, Zhaojun Wang et al.
Molecules
Proteins in Food Systems
article

Effects of Thermal Denaturation on the Interactions Between Soluble Soybean Polysaccharides and Casein and Whey Protein

Hongyang Pan, Shenghu Zhou, Xiaofang Chu, Zhaojun Wang, Jie Chen
article en

Abstract

This study aimed to investigate the interactions between soluble soybean polysaccharides (SSPS) and milk proteins, namely, casein and whey protein, and to evaluate their effects on the stability of acidified milk beverages under different degrees of thermal denaturation. Casein, whey protein, and SSPS were used as raw materials to prepare mixed solutions under varying pH conditions. A combination of analytical techniques, including centrifugal sedimentation rate, particle size distribution, ζ-potential measurement, differential scanning calorimetry (DSC), size-exclusion chromatography (SEC), and LUMisizer stability analysis, was employed to systematically examine the interactions between SSPS and the two proteins, as well as the influence of thermal treatment at 120-140 °C (casein) and 65-78 °C (whey protein). The results demonstrated that under acidic conditions (pH 3.5-4.5), SSPS formed compact complexes with casein, effectively stabilizing casein dispersions through steric hindrance and electrostatic repulsion. In contrast, SSPS exhibited a limited stabilizing ability toward whey protein due to its strong tendency to aggregate, which hindered the formation of uniform complexes. Regarding thermal denaturation, casein heated at 140 °C for more than 40 min showed pronounced κ-casein dissociation and aggregation, resulting in reduced stability of the SSPS-casein system. For whey protein, increasing thermal denaturation (complete denaturation at 78 °C for 30 min) led to the formation of larger aggregates, with particle size increasing from 198.23 nm to 213.33 nm and ζ-potential decreasing from -3.77 mV to -2.01 mV, thereby diminishing the stability of the SSPS-whey protein system. Overall, this study elucidates the interaction mechanisms of SSPS with casein and whey protein, and highlights the role of thermal denaturation, thereby providing theoretical guidance for the effective application of SSPS in acidified milk beverages.

MoleculesVol. 30(21)
Jiangnan University (CN), Chinese Academy of Sciences (CN), State Key Laboratory of Food Science and Technology (CN), Institute of Botany (CN)
Openalex Percentile: Top 63%
Proteins in Food Systems
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