2022
DOI: 10.1016/j.colsurfa.2022.128267
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Structure-property relations of β-lactoglobulin/κ-carrageenan mixtures in aqueous foam

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Cited by 12 publications
(7 citation statements)
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“…The foaming capacity and stability were observed to be 61.35% and 65.32%, respectively. The foaming ability of SISH depended on a variety of conditions, including their structure, molecular weight, protein and carbohydrate content, and the presence of other agents [ 34 , 35 ]. The interfacial characteristics of hydrocolloids can be directly correlated with their high protein concentration [ 36 ].…”
Section: Resultsmentioning
confidence: 99%
“…The foaming capacity and stability were observed to be 61.35% and 65.32%, respectively. The foaming ability of SISH depended on a variety of conditions, including their structure, molecular weight, protein and carbohydrate content, and the presence of other agents [ 34 , 35 ]. The interfacial characteristics of hydrocolloids can be directly correlated with their high protein concentration [ 36 ].…”
Section: Resultsmentioning
confidence: 99%
“…There are many factors that affect the elastic modulus change of the system during heating, such as composition, heating rate, and salt ion effect. [ 4 , 32 ] Batter as a mixed system, during this experiment, is only affected by EY pollution and enzymatic hydrolysis, indicating that the density change caused by air mixing is the most prominent influence on the batter properties. Therefore, it is speculated that less air mixing is not conducive to the formation of network structure during the heating process of cake, and the inability to form mature network structures at higher temperatures may also cause gas expansion escape.…”
Section: Resultsmentioning
confidence: 83%
“…Both the foam stability and quality are closely related to the interfacial properties of the foam. Properties of the interfacial layers are governed by their composition and structure, but also to a large extent by interfacial intermolecular interactions such as repulsive electrostatic as well as attractive hydrophobic interactions [ 4 ]. Egg white (EW) protein has suitable amphiphilic property, which is conducive to its air expansion to form foam and maintain a stable structure.…”
Section: Introductionmentioning
confidence: 99%
“…If the charge density, surface tension, dilatational rheology, and foam properties of WPI are known, the changes in its stability can be obtained using dilatational rheology-property relationship. This has been recently demonstrated with β-lactoglobulin/kappa-carrageenan (κC) foams (Rafe, Glikman, et al, 2022).…”
Section: Introductionmentioning
confidence: 88%