“…This enhancement can be attributed to ultrasonic treatment, which unfolds the hydrophobic structure of protein molecules and release-free sulfhydryl groups, thus promoting the connection of XG and QPI molecules to form a more stable chain group structure. At pH 4.5, near the protein's isoelectric point, protein aggregation and insufficient QPI and XG binding lead to heterogeneity, mirroring the findings from Yang's research on heat-induced gels and the ultrasonic treatment of soy protein [41]. The observation that G ′ displayed frequency dependence, whereas G ′′ remained relatively unaffected by frequency changes, aligns with the literature, indicating that food gels, as viscoelastic materials, typically show such behavior [42].…”
The properties of xanthan gum protein gels composed of quinoa protein (XG-QPG) and ultrasound-treated quinoa protein (XG-UQPG) were compared for the preparation of high-quality quinoa protein gels. The gel qualities at different pH values were compared. The gels were used to produce eggless bread. Microscopically, the secondary structure of the proteins in XG-QPG (pH 7.0) was mainly α-helix, followed by random coiling. In contrast, the content of β-sheet in XG-UQPG was higher, relative to the viscoelastic properties of the gel. Moreover, the free sulfhydryl groups and disulfide bonds of XG-QPG (pH 7.0) were 48.30 and 38.17 µmol/g, while XG-UQPG (pH 7.0) was 31.95 and 61.58 µmol/g, respectively. A high disulfide bond content was related to the formation of gel networks. From a macroscopic perspective, XG-QPG (pH 7.0) exhibited different pore sizes, XG-UQPG (pH 7.0) displayed a loose structure with uniform pores, and XG-UQPG (pH 4.5) exhibited a dense structure with small pores. These findings suggest that ultrasound can promote the formation of a gel by XG-UQPG (pH 7.0) that has a loose structure and high water-holding capacity and that XG-UQPG (pH 4.5) forms a gel with a dense structure and pronounced hardness. Furthermore, the addition of the disulfide bond-rich XG-UQPG (pH 7.0) to bread promoted the formation of gel networks, resulting in elastic, soft bread. In contrast, XG-UQPG (pH 4.5) resulted in firm bread. These findings broaden the applications of quinoa in food and provide a good egg substitute for quinoa protein gels.
“…This enhancement can be attributed to ultrasonic treatment, which unfolds the hydrophobic structure of protein molecules and release-free sulfhydryl groups, thus promoting the connection of XG and QPI molecules to form a more stable chain group structure. At pH 4.5, near the protein's isoelectric point, protein aggregation and insufficient QPI and XG binding lead to heterogeneity, mirroring the findings from Yang's research on heat-induced gels and the ultrasonic treatment of soy protein [41]. The observation that G ′ displayed frequency dependence, whereas G ′′ remained relatively unaffected by frequency changes, aligns with the literature, indicating that food gels, as viscoelastic materials, typically show such behavior [42].…”
The properties of xanthan gum protein gels composed of quinoa protein (XG-QPG) and ultrasound-treated quinoa protein (XG-UQPG) were compared for the preparation of high-quality quinoa protein gels. The gel qualities at different pH values were compared. The gels were used to produce eggless bread. Microscopically, the secondary structure of the proteins in XG-QPG (pH 7.0) was mainly α-helix, followed by random coiling. In contrast, the content of β-sheet in XG-UQPG was higher, relative to the viscoelastic properties of the gel. Moreover, the free sulfhydryl groups and disulfide bonds of XG-QPG (pH 7.0) were 48.30 and 38.17 µmol/g, while XG-UQPG (pH 7.0) was 31.95 and 61.58 µmol/g, respectively. A high disulfide bond content was related to the formation of gel networks. From a macroscopic perspective, XG-QPG (pH 7.0) exhibited different pore sizes, XG-UQPG (pH 7.0) displayed a loose structure with uniform pores, and XG-UQPG (pH 4.5) exhibited a dense structure with small pores. These findings suggest that ultrasound can promote the formation of a gel by XG-UQPG (pH 7.0) that has a loose structure and high water-holding capacity and that XG-UQPG (pH 4.5) forms a gel with a dense structure and pronounced hardness. Furthermore, the addition of the disulfide bond-rich XG-UQPG (pH 7.0) to bread promoted the formation of gel networks, resulting in elastic, soft bread. In contrast, XG-UQPG (pH 4.5) resulted in firm bread. These findings broaden the applications of quinoa in food and provide a good egg substitute for quinoa protein gels.
“…5 B) and SH contents ( Fig. 6 C), and the exposure of hydrophobic groups drives the molecules to engage in intermolecular interactions, through disulfide bonds and hydrophobic interactions, resulting in the formation of a homogeneous gel network [32] , [33] . Fig.…”
“…The most superior SPH gel was formed at pH 7 than acidic and alkaline conditions [43] Peanut protein isolate Gel properties and protein structure pH-shifting (2,4,10,12) Gel strength of PPI10 were significantly improved [18] Soy protein isolate Textural properties Extreme acid pH-shifting (1.5) SPI structural unravelling at acidic pH-shifting [35] Soy protein isolate Textural properties Preheating treatment (70-100 • C)…”
Section: Sample Aim Of the Study Influence Factor Results Referencesmentioning
With increasing awareness of human health, proteins from plant sources are being considered as alternatives to those from animal sources. The market for plant-based meat substitutes is expanding to satisfy the growing consumer demand. However, the functional properties of natural proteins frequently do not satisfy the needs of the modern food industry, which requires high-quality properties. Research on improving the functional properties of proteins is currently a popular topic. Based on the gel properties of proteins, this study focused on the formation mechanism of heat-induced protein gels, which will be helpful in expanding the market for plant protein gel products. Regulatory strategies for heat-induced gels were reviewed, including protein composition, pH, ionic strength, other food components, and processing techniques. The effects of other food components (such as polysaccharides, proteins, polyphenols, and liposomes) are discussed to provide insights into the properties of plant protein gels. Studies have shown that these factors can effectively improve the properties of plant protein gels. In addition, the development and application potential of emerging processing technologies that can contribute to safe and effective applications in actual food production are discussed. For the future, plant protein gels are playing an irreplaceable role in the new direction of future food.
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