2016
DOI: 10.1016/j.foodhyd.2016.01.005
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Identification of critical concentrations determining foam ability and stability of β-lactoglobulin

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Cited by 36 publications
(38 citation statements)
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“…Herein, the time-dependent development of the surface pressure is indicative of a decrease in surface tension and yields information about the adsorption behavior of proteins. The surface pressure was plotted as a function of the square root of the adsorption time to better illustrate differences in the adsorption rate between samples [27,28]. The surface pressure and the adsorption rate of the untreated insoluble microalgae protein increased with increasing concentration (Fig.…”
Section: Resultsmentioning
confidence: 99%
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“…Herein, the time-dependent development of the surface pressure is indicative of a decrease in surface tension and yields information about the adsorption behavior of proteins. The surface pressure was plotted as a function of the square root of the adsorption time to better illustrate differences in the adsorption rate between samples [27,28]. The surface pressure and the adsorption rate of the untreated insoluble microalgae protein increased with increasing concentration (Fig.…”
Section: Resultsmentioning
confidence: 99%
“…The critical protein concentration has been defined as the concentration at which the surface pressure becomes independent of the surfactant concentration, and can be obtained from adsorption equilibrium plots i.e. the concentration where a plateau region begins [28,34]. To that purpose, we plotted the equilibrium surface pressure as a function of the protein concentration (Fig.…”
Section: Resultsmentioning
confidence: 99%
“…Furthermore, it was shown that the ionic strength affects the association state of glycinin (43). At pH 7.6 and I = 0.5 M, glycinin is present as hexamer (45,46), whereas at I = 0.03 M it is predominantly present as hexamer, while a small part of it (15-20%) is present as trimer (43). Thus, the ionic strength of the system is of importance especially when multimeric proteins, e.g.…”
Section: Solubilitymentioning
confidence: 99%
“…With respect to Rubisco, to our knowledge, there is no literature available regarding the effect of ionic strength on the association/dissociation state of the protein. Typically, urea (47) or SDS (48) are applied to effectively dissociate Rubisco into its subunits.…”
Section: Solubilitymentioning
confidence: 99%
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