Heat-induced aggregation of subunits/polypeptides of soybean protein: Structural and physicochemical properties

Ju, Qian; Yuan, Yanqiu; Wu, Chang; Hu, Yayun; Zhou, Shuyi; Luan, Guangzhong

doi:10.1016/j.foodchem.2022.134774

Cited by 24 publications

(3 citation statements)

References 39 publications

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“…These results suggest that alkali extraction and acid precipitation had minimal impact on the conformation of the 7S and 11S globulins, as well as the limited exposure of hydrophobic groups for bromophenol blue binding. During heat treatment, protein aggregation involves intricate intermolecular interactions, primarily driven by hydrophobic associations [ 25 ]. Elevated temperatures affected protein conformation, leading to the increased exposure of hydrophobic groups and binding sites, thereby promoting intermolecular hydrophobic association [ 26 ].…”

Section: Resultsmentioning

confidence: 99%

“…As depicted in Figure 3 , the viscosity levels of the three ratios of proteins were all below 50 mPa·s at the initial temperature of 25 °C. With increasing temperature, the viscosities of proteins at different proportions exhibited a significant increase, indicating conformational changes primarily attributed to thermal denaturation temperatures [ 25 ]. Upon heating the samples to 85 °C for 15 min and subsequent cooling to 25 °C, the viscosities of proteins at various proportions continued to rise.…”

Section: Resultsmentioning

confidence: 99%

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Effect of Thermal Treatment on Gelling and Emulsifying Properties of Soy β-Conglycinin and Glycinin

Zhang,

Jin,

Wang

et al. 2024

Foods

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This study investigated the impact of different preheat treatments on the emulsifying and gel textural properties of soy protein with varying 11S/7S ratios. A mixture of 7S and 11S globulins, obtained from defatted soybean meal, was prepared at different ratios. The mixed proteins were subjected to preheating (75 °C, 85 °C, and 95 °C for 5 min) or non-preheating, followed by spray drying or non-spray drying. The solubility of protein mixtures rich in the 7S fraction tended to decrease significantly after heating at 85 °C, while protein mixtures rich in the 11S fraction showed a significant decrease after heating at 95 °C. Surprisingly, the emulsion stability index (ESI) of protein mixtures rich in the 7S fraction significantly improved twofold during processing at 75 °C. This study revealed a negative correlation between the emulsifying ability of soy protein and the 11S/7S ratio. For protein mixtures rich in either the 7S or the 11S fractions, gelling proprieties as well as emulsion activity index (EAI) and ESI showed no significant changes after spray drying; however, surface hydrophobicity was significantly enhanced following heating at 85 °C post-spray drying treatment. These findings provide insights into the alterations in gelling and emulsifying properties during various heating processes, offering great potential for producing soy protein ingredients with enhanced emulsifying ability and gelling property. They also contribute to establishing a theoretical basis for the standardized production of soy protein isolate with specific functional characteristics.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Effect of Thermal Treatment on Gelling and Emulsifying Properties of Soy β-Conglycinin and Glycinin

Zhang,

Jin,

Wang

et al. 2024

Foods

View full text Add to dashboard Cite

show abstract

“…The Ellman reagent method was used with minor modifications (Figueroa‐González et al ., 2022; Ju et al ., 2023). First, freeze‐dry the working solution in 2.3.…”

Section: Methodsmentioning

confidence: 99%

Effect of pH on the structure and emulsification properties of ultrasonicated water‐soluble protein from Moringa oleifera seed

Tang,

Du,

et al. 2023

Int J of Food Sci Tech

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SummaryThe Moringa seed protein (MOS) is a new protein resource, the development and utilisation of MOS is still in its early stages due to the late introduction of its varieties. To improve the range of available MOS protein, this study investigated the effects of different pH levels on the ultrasonic modification of MOS protein (UMOWP), exploring the feasibility of UMOWP emulsion systems in food. The zeta potential analysis revealed that the isoelectric point (pI) of UMOWP was 5.8. The secondary structures of UMOWP could be regulated by pH. Moreover, different secondary structures led to different tertiary structures and chemical bonds in UMOWP. Compared with pH values near pI, surface hydrophobicity significantly increased but the total S–S group and particle size decreased away from pI. Furthermore, UMOWP partially dissociated at pH 3, and the degree of dissociation was weaker at pH 9 and pH 11. These structural changes led to significant improvements in the emulsification properties of UMOWP at pH 11, resulting in better environmental stability of the emulsion. These findings provide a foundation for the potential application of MOS proteins in the food industry.

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The influence of α and α′ subunits on SPI Pickering emulsions based on natural hybrid breeding varieties

Gu,

Dong,

Jiang

et al. 2023

Food Chemistry: X

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Heat-induced aggregation of subunits/polypeptides of soybean protein: Structural and physicochemical properties

Cited by 24 publications

References 39 publications

Effect of Thermal Treatment on Gelling and Emulsifying Properties of Soy β-Conglycinin and Glycinin

Effect of Thermal Treatment on Gelling and Emulsifying Properties of Soy β-Conglycinin and Glycinin

Effect of pH on the structure and emulsification properties of ultrasonicated water‐soluble protein from Moringa oleifera seed

The influence of α and α′ subunits on SPI Pickering emulsions based on natural hybrid breeding varieties

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