2020
DOI: 10.1016/j.foodhyd.2020.105978
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Phase separation behavior and characterization of ovalbumin and propylene glycol alginate complex coacervates

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Cited by 68 publications
(32 citation statements)
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“…In fact, as the number of available OPI molecules increased on the GA chain, each protein molecule might have not needed a large number of positive charges to form complexes with the polysaccharide molecules. [10] In contrast, when the mixing ratio was increased, pH ϕ2 remained constant. As Figure 6b shows, the maximum OD and, the largest amount of the complex was formed at the OPI: GA mixing ratio of 4:1, which indicated the protein was saturated with GA.; thus, the 4:1 OPI: GA mixture was selected for further evaluation.…”
Section: State Diagrammentioning
confidence: 99%
See 1 more Smart Citation
“…In fact, as the number of available OPI molecules increased on the GA chain, each protein molecule might have not needed a large number of positive charges to form complexes with the polysaccharide molecules. [10] In contrast, when the mixing ratio was increased, pH ϕ2 remained constant. As Figure 6b shows, the maximum OD and, the largest amount of the complex was formed at the OPI: GA mixing ratio of 4:1, which indicated the protein was saturated with GA.; thus, the 4:1 OPI: GA mixture was selected for further evaluation.…”
Section: State Diagrammentioning
confidence: 99%
“…et al (2020) who reported that ovalbumin and propylene glycol alginate complex coacervates showed higher thermal stability than the protein alone. [10] TGA was used to better evaluate the thermal properties of the complex as shown in Figure 9b. Both the endothermic and exothermic processes had ranges of temperature near the range recorded during the TGA weight loss step.…”
Section: Thermal Behaviormentioning
confidence: 99%
“… Principal strategies used to create polysaccharide-based materials by physical association for biomedical applications. Adapted with permission from References [ 139 , 140 , 141 , 142 , 143 , 144 , 145 ]; published by Elsevier, 2019, 2020, 2018, 2020, 2020, 2010, and 2020, respectively. Adapted with permission from Reference [ 146 ]; published by American Chemical Society, 2020.…”
Section: Figurementioning
confidence: 99%
“…Generally speaking, the interactions between proteins and polysaccharides can be associative or segregative [ 4 ]. When proteins and polysaccharides have opposite charges, associative electrostatic interactions make proteins and polysaccharides easily form complexes through electrostatic attraction [ 3 , 5 ]. It was also found that when both biopolymers were net-negatively charged, complexes could still form [ 3 ].…”
Section: Introductionmentioning
confidence: 99%
“…It was also found that when both biopolymers were net-negatively charged, complexes could still form [ 3 ]. The formed biopolymers still have complex coacervation behaviors, which are mainly determined by the electrostatic interactions, such as molecular properties (charge density and size), environmental factors (pH, mixing ratio of proteins and polysaccharides, salt, total concentration of biological macromolecules and temperature) and other factors (shear rate) [ 5 , 6 ].…”
Section: Introductionmentioning
confidence: 99%