Correlating structure and emulsification of soybean protein isolate: Synergism between low-pH-shifting treatment and ultrasonication improves emulsifying properties

Liu, Guannan; Hu, Miao; Du, Xiaoqian; Liao, Yi; Yan, Shizhang; Zhang, Shuang; Qi, Baokun; Li, Yang

doi:10.1016/j.colsurfa.2022.128963

Cited by 30 publications

(15 citation statements)

References 52 publications

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“…1 A, the peak at 3285.14 cm −1 is linked to the stretching vibration of the intermolecular hydrogen bond between O—H and N—H. The change in the peak position indicates that ultrasound and pH shifting caused a change in the number of intramolecular hydrogen bonds [11] . The peak value of the amide I band moved from 1653.14 to 1668.18 cm −1 after combined pH-shifting and ultrasound treatment, indicating rearrangement of the protein–peptide chain or a change in the secondary structure, which altered the peak amide I band in 7S [32] .…”

Section: Resultsmentioning

confidence: 98%

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Molecular structural modification of β-conglycinin using pH-shifting with ultrasound to improve emulsifying properties and stability

Yang

Lian

Wang

et al. 2022

Ultrasonics Sonochemistry

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Section: Resultsmentioning

confidence: 98%

“…However, the improvement in protein emulsifying properties through pH-shifting is limited [11] , therefore, there is a need to use other approaches to further modify proteins. Being a green, simple, and promising modification modality, ultrasound is widely used to change the functional properties of proteins [12] .…”

Section: Introductionmentioning

confidence: 99%

Molecular structural modification of β-conglycinin using pH-shifting with ultrasound to improve emulsifying properties and stability

Yang

Lian

Wang

et al. 2022

Ultrasonics Sonochemistry

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“…As shown in Figure 9 b, the ESI of gluten was significantly lower than that of the Glu-KGM mixtures and conjugates. Therefore, the Glu-KGM conjugates could form an interface film and promote the dispersion of oil droplets, which was the result of the unfolding of the conjugates structures [ 35 ]. The ESI values of the Glu-KGM conjugates increased with the increase in reaction time.…”

Section: Resultsmentioning

confidence: 99%

Physicochemical and Structural Properties of Gluten-Konjac glucomannan Conjugates Prepared by Maillard Reaction

et al. 2023

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Gluten (Glu) is important to wheat products by forming a three-dimensional matrix. This study aimed to investigate the physicochemical and structural properties of gluten after conjugation with konjac glucomannan (KGM) through the Maillard reaction. The study revealed that the degree of graft increased with the prolonged reaction time. The Glu-KGM conjugates were possessed of increased β-sheet but decreased α-helix and β-turn, as well as unfolding and loose tertiary structures as the reaction proceeded. Among three different proportions, the Glu-KGM 1:1 conjugate was proved to have the most excellent foaming and emulsifying properties, and could form more rigid and firm gelation structures, which could be related to the decreased particle size and increased zeta potential of the conjugate. Overall, the physicochemical and structural properties of gluten were significantly related to the KGM ratios as well as the reaction period.

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“…The sonication process can change the secondary structure of proteins and reduce their size. It further extends their techno‐functionality, such as molecular flexibility, surface charge, interfacial adsorption, and solubility, leading to better emulsifying ability and stability with smaller oil droplet sizes (Liu, Hu, Du, Liao, et al, 2022; Mozafarpour, Koocheki, & Nicolai, 2022; Mozafarpour, Sani, Koocheki, McClements & Mehr, 2022; Xu et al, 2021; Zhang, Liu, et al, 2022; Zhi et al, 2022). Mekala et al (2022a) observed larger oil droplets in US‐treated lentil protein concentrate (LPC) emulsions.…”

Section: Physical Modificationsmentioning

confidence: 99%

Recent advances in legume protein‐based colloidal systems

Tarahi

Ahmed

2023

Legume Science

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Developing nature‐derived surface‐active ingredients with favorable interfacial and functional properties has recently received increasing attention in the food and pharmaceutical industries. Legume proteins are used extensively in food colloidal systems because of their small particle size, high water absorption capability, excellent functional properties (e.g., emulsification, foamability, and gelation), and film formation. There are some limitations in legume proteins, such as high water vapor permeability and fragility, as well as low stability and solubility. Various conventional and innovative processing technologies (e.g., high‐pressure homogenization, ultrasonication, and cold plasma processing) have been successfully employed in order to modify the functional and interfacial properties of legume proteins. In this review, the formation and stability of legume protein‐based colloidal systems and their applications are discussed.

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Correlating structure and emulsification of soybean protein isolate: Synergism between low-pH-shifting treatment and ultrasonication improves emulsifying properties

Cited by 30 publications

References 52 publications

Molecular structural modification of β-conglycinin using pH-shifting with ultrasound to improve emulsifying properties and stability

Molecular structural modification of β-conglycinin using pH-shifting with ultrasound to improve emulsifying properties and stability

Physicochemical and Structural Properties of Gluten-Konjac glucomannan Conjugates Prepared by Maillard Reaction

Recent advances in legume protein‐based colloidal systems

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