Unexpected differences in the behavior of ovotransferrin at the air–water interface at pH 6.5 and 8.0

Floch-Fouéré, Cécile Le; Pezennec, Stéphane; Pézolet, Michel; Rioux-Dubé, Jean-François; Renault, Anne; Beaufils, Sylvie

doi:10.1016/j.jcis.2011.01.073

Cited by 10 publications

(9 citation statements)

References 68 publications

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“…Values of C 0 in citrate and in acetate are similar (0.92 and 0.78 mg m À2 respectively) which is consistent with values of several proteins lie between 0.1 and 1.2 mg m À2 [44]. It is the case for ovotransferrin at pH 6.5 and at pH 8.0 (0.77 and 0.45 mg m À2 respectively) [33].…”

Section: In the First Steps Of Adsorption Citrate Favors Interfacial supporting

confidence: 80%

“…At pH 4.0 in acetate, kinetics of adsorption for a bulk ovotransferrin concentration of 100 lg mL À1 are typical for globular proteins and comparable with those obtained with ovalbumin [22] and ovotransferrin [33]. A final plateau value close to 12°is rapidly reached during the adsorption kinetics which is consistent with the formation of a saturated monolayer [22,26,31,41,42].…”

Section: Interfacial Heterogeneity In the Presence Of Citratesupporting

confidence: 65%

“…3). For comparison, values obtained for ovotransferrin at pH 6.5 and 8.0 at this concentration are close to 18 mN m À1 [33]. However, if the final value is the same, kinetics of surface pressure are different on shorter time.…”

Section: Interfacial Heterogeneity In the Presence Of Citratementioning

confidence: 60%

“…In a previous work [33], we have investigated the adsorption behavior of apo-ovotransferrin and its interfacial properties at its iso-electric pH (pH 6.5) and in conditions of negative net charge (pH 8.0), in a four-decade concentration range. We have reported that no significant difference was observed between pH 6.5 and 8.0 as regards the final value of surface concentration and surface pressure.…”

Section: Introductionmentioning

confidence: 99%

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Moderate conformational impact of citrate on ovotransferrin considerably increases its capacity to self-assemble at the interface

Floch-Fouéré

Pezennec

Pasco

et al. 2015

Journal of Colloid and Interface Science

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We have compared the behavior of ovotransferrin at the air-solution interface in the presence of a monovalent ion (acetate), or a divalent ion (citrate), the latter being known to induce conformational changes of this protein upon interaction with its iron-binding sites. We have characterised the adsorption layer at the air-water interface in terms of homogeneity, surface concentration excess and rheological properties at pH 4.0. Besides we have investigated the bulk conformation in the presence of the two anions. In the presence of citrate only, interfacial layers display well-defined domains of higher overall surface concentration suggesting multilayers adsorption. Citrate also induces higher helical content and stabilizes the protein against thermal denaturation. Hence we propose that these changes are involved in the propensity of ovotransferrin to self-assemble at the air-water interface resulting in thick and heterogeneous interfacial layer.

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Section: In the First Steps Of Adsorption Citrate Favors Interfacial supporting

confidence: 80%

Section: Interfacial Heterogeneity In the Presence Of Citratesupporting

confidence: 65%

Section: Interfacial Heterogeneity In the Presence Of Citratementioning

confidence: 60%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Moderate conformational impact of citrate on ovotransferrin considerably increases its capacity to self-assemble at the interface

Floch-Fouéré

Pezennec

Pasco

et al. 2015

Journal of Colloid and Interface Science

Self Cite

View full text Add to dashboard Cite

show abstract

“…Increasing the exposed hydrophobicity of proteins by means of conjugation with lipid chains was shown to increase the adsorption rate to the air-water interface . Net charge is a second parameter of interest determining adsorption kinetics, in which higher net charge slows down the adsorption process due to the electric repulsive forces involved Kudryashova et al, 2005;Le Floch-Fouéré et al, 2011). Highly aggregated heat-treated ovalbumin was further shown to induce a ten-fold decrease the diffusion rate of proteins to the interface compared to the native protein (Kudryashova et al, 2005).…”

Section: Foamsmentioning

confidence: 99%