Phase behavior, thermodynamic and rheological properties of ovalbumin/dextran sulfate: Effect of biopolymer ratio and salt concentration

Liu, Jingbo; Chai, Jiale; Zhang, Ting; Yang, Yuchong; Saini, Ramesh Kumar; Xu, Meng-Lei; Li, Shanle; Shang, Xiaomin

doi:10.1016/j.foodhyd.2021.106777

Cited by 34 publications

(16 citation statements)

References 49 publications

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“…When the mixing ratio of APs/WPI greater than 1:4, the turbidity increased within a narrow range, suggesting that the number of APs chains was in an excessive state. A similar phenomenon was reported for ovalbumin-XG and lysozyme-XG [49]. In addition, the increasing ratio of APs/WPI from 1:9 to 3:1 favors the formation of the APs-WPI complex due to the lower amounts of WPI molecules in the APs-WPI complexes at a higher mixing ratio.…”

Section: The Chemical Composition Of Aps and Effect Of Ph Value On Wp...supporting

confidence: 81%

Effects of biopolymer ratio and pH value on the complex formation between whey protein isolates and soluble Auricularia auricular polysaccharides

Li¹,

Shao‐Horn²,

Han³

et al. 2023

Food Science of Animal Products

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Biopolymer complexes fabricated by proteins and neutral polysaccharides have some specific and innovative functionalities. A better understanding of the interactions among these biopolymers might provide new insight into the applications of the complexes. Therefore, this study aimed to investigate the structural characteristics and molecular interaction mechanisms of whey protein isolates (WPI) and Auricularia auricular polysaccharides (APs). The turbidity analysis confirmed that the pH value and mixing ratio of the two polymers had strong effects on the formation of the APs-WPI complexes. All dispersions formed soluble complexes at approximately pH = 6.0 (pH c ). APs-WPI self-assembles exhibited physically cross-linked networks under higher APs proportions, while they formed spherical complexes at higher WPI ratios. The addition of APs could alter the secondary structure of WPI, and the most noticeable changes were located in the regions of β-sheet and β-turn as confirmed by circular dichroism (CD) analysis. A molecular docking study showed that the amino acid residues of β-lactoglobulin complexed with the -COOH and -OH groups of APs. Hydrogen bonds and hydrophobic interactions, which were nonbonding contributions, played a key role in the formation of the APs-WPI complex. This study provided a basis for the development and application of APs in WPI-based beverages.

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Section: The Chemical Composition Of Aps and Effect Of Ph Value On Wp...supporting

confidence: 81%

Effects of biopolymer ratio and pH value on the complex formation between whey protein isolates and soluble Auricularia auricular polysaccharides

Li¹,

Shao‐Horn²,

Han³

et al. 2023

Food Science of Animal Products

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“…1D), the frequency of contact between droplets increased, further leading to an augment in G ' and G " 47 . The growth of G " indicated that the solution formed an interlinked gel‐like network structure that was relatively prone to denaturation and aggregation at the initial stage of gelation 16 . In addition, G ' was higher than G " throughout the experiment, revealing that the EWP solution was a strong gel system with good elastic behavior 48 .…”

Section: Resultsmentioning

confidence: 97%

“…47 The growth of G" indicated that the solution formed an interlinked gel-like network structure that was relatively prone to denaturation and aggregation at the initial stage of gelation. 16 In addition, G' was higher than G" throughout the experiment, revealing that the EWP solution was a strong gel system with good elastic behavior. 48 Tan ⊐ decreased at the beginning of storage and then increased at all three conditions (-20, 4 and 25 °C), except at 37 °C during the 60-day storage period.…”

Section: Rheological Properties Of Ewp Solutionmentioning

confidence: 95%

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Storage impact on egg white powder's physical and functional properties

Zhang

Tang

et al. 2022

J Sci Food Agric

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BACKGROUND Changes in storage temperature and time alter the functional properties of egg white powder (EWP) and determine its quality and shelf‐life, finally affecting the consumer acceptance of the products made from EWP. In the present study, the EWP samples were stored at four different temperatures (−20, 4, 25 and 37 °C) for 60 days, and then the protein structural, physical and functional properties of EWP were measured and assessed further for correlation with storage conditions using heatmap. RESULTS The viscosity of the EWP solution increased after 30 days. Foaming ability and rheological properties increased first and then decreased compared to untreated samples with the prolonged storage time. Correlation analysis results indicated that the gel hardness, water holding capacity, foaming ability, emulsifying ability, particle size, dispersibility and viscosity of EWP were significantly related to storage time (P < 0.05). Only the gelation properties of EWP stored at 37 °C for 60 days changed significantly and were negatively related to its moisture content (P < 0.05). Additionally, the random coil content of EWP was positively correlated with particle size, moisture content, solubility and gel properties, whereas β‐sheet was negatively correlated with them. CONCLUSION Compared to other temperatures, the functional properties of EWP were relatively stable under 4 °C. Therefore, the low temperature (4 °C) was selected as the most suitable storage temperature for EWP. The results of the present study could provide a theoretical basis for the shelf‐life extension of EWP. © 2022 Society of Chemical Industry.

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“…[ 45,47,[58][59][60][61][62][63][64][65][66][67][68][69][70][71][72] Entropy gain dominated complex coacervation (ΔH > 0, ΔS > 0)…”

Section: Underlying Mechanismmentioning

confidence: 99%

New insights into protein–polysaccharide complex coacervation: Dynamics, molecular parameters, and applications

Zheng,

Van der Meeren,

Sun

2023

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For more than a decade, the discovery of liquid–liquid phase separation within living organisms has prompted colloid scientists to understand the connection between coacervate functionality, phase behavior, and dynamics at a multidisciplinary level. Although the protein–polysaccharide was the first system in which the coacervation phenomenon was discovered and is widely used in food systems, the phase state and relaxation dynamics of protein–polysaccharide complex coacervates (PPCC) have rarely been discussed previously. Consequently, this review aims to unravel the relationship between PPCC dynamics, thermodynamics, molecular architecture, applications, and phase states in past studies. Looking ahead, solving the way molecular architecture spreads to macro‐functionality, that is, establishing the relationship between molecular architecture–dynamics–application, will catalyze novel advancements in PPCC research within the field of foods and biomaterials.

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Phase behavior, thermodynamic and rheological properties of ovalbumin/dextran sulfate: Effect of biopolymer ratio and salt concentration

Cited by 34 publications

References 49 publications

Effects of biopolymer ratio and pH value on the complex formation between whey protein isolates and soluble Auricularia auricular polysaccharides

Effects of biopolymer ratio and pH value on the complex formation between whey protein isolates and soluble Auricularia auricular polysaccharides

Storage impact on egg white powder's physical and functional properties

New insights into protein–polysaccharide complex coacervation: Dynamics, molecular parameters, and applications

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