Interfacial properties of acidified skim milk

Cases, Eliane; Rampini, C; Cayot, Ph.

doi:10.1016/j.jcis.2004.08.115

Cited by 32 publications

(24 citation statements)

References 59 publications

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“…As the hydroxyapatite surface is also positively charged at the pH values used in this study, electrostatic interactions between casein and hydroxyapatite are unlikely, but our results indicate that adsorption occurs nonetheless. This is perhaps driven mainly by hydrophobic interactions, in agreement with the enhancement of casein adsorption at an oil-water interface at low pH (35).…”

Section: Discussionsupporting

confidence: 73%

Inhibition of hydroxyapatite dissolution by whole casein: the effects of pH, protein concentration, calcium, and ionic strength

Barbour

Shellis

Parker

et al. 2008

European J Oral Sciences

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Formulating drinks with reduced erosive potential is one approach for reducing dental erosion. In this study, whole casein was added to citric acid solutions representative of soft drinks, and the hydroxyapatite dissolution rate was assessed. Adding 0.02% (w/v) casein to acid solutions significantly reduced the hydroxyapatite dissolution rate by 51 +/- 4% at pH values of 2.80, 3.00, 3.20, 3.40, and 3.60, although the baseline dissolution rates of course varied as a function of pH. The protein concentration [0.002, 0.02, and 0.2% (w/v) casein] had no significant effect on dissolution inhibition. Adding both casein and calcium to citric acid resulted in a further reduction in the dissolution rate at low and intermediate calcium concentrations (5 and 10 mM) but not at higher calcium concentrations (20 and 50 mM). Ionic strength had no significant impact on the efficacy of casein. Casein also significantly reduced the hydroxyapatite dissolution rate when the hydroxyapatite was coated with a salivary pellicle. The reduction in dissolution rate is ascribed to firmly adsorbed casein on the hydroxyapatite surface, which stabilizes the crystal surface and inhibits ion detachment.

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Section: Discussionsupporting

confidence: 73%

Inhibition of hydroxyapatite dissolution by whole casein: the effects of pH, protein concentration, calcium, and ionic strength

Barbour

Shellis

Parker

et al. 2008

European J Oral Sciences

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“…This second stage would correspond to a slow unfolding and molecular rearrangement such as intermolecular association or aggregation of the individual unfolded protein molecules at the interface. As consequence of these structural modifications, additional protein layers could be formed 21 and a continuous membrane can take place at the oil-water interface 25 . As shown Figure 1 (curve 2), under acidic condition, pea protein exhibited a slower lowering of the interfacial tension and adsorption equilibrium is reached after about 8,000 s. The initial slope dγ/dt (extracted from Figure 1) were significantly affected depending on the pH value and results showed that the initial slope dγ/dt developed by pea protein at pH 2.4 was inhibited dg=dt j j$ 4:67 Â 10 À3 mNm À1 s À1 À Á as compared to pH 7.0 dg=dt j j$ 23:33 Â 10 À3 mNm À1 s À1 À Á .…”

Section: Resultsmentioning

confidence: 99%

“…The variation amplitude of area is 10%. Measurements were carried out as previously described by 21 . Under these conditions and for a concentration of pea protein isolate of 0.04 wt.%, the interface was fully covered and only a very small amount of protein remained in the bulk phase 22 necessary for the clarity of the medium.…”

Section: Interfacial Propertiesmentioning

confidence: 99%

Interfacial and Emulsifying Characteristics of Acid-treated Pea Protein

et al. 2009

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This work presents equilibrium and dynamic aspects for the adsorption at the oil-water interface of pea (Pisum sativum L.) protein isolate (PPI). Dynamic interfacial tension, γ, and surface viscoelasticity modulus, ε, were determined using pendant-drop method. Adsorption kinetics studies revealed that pea proteins adsorb faster at pH 7.0 than at acidic pH (pH 2.4). On the other hand, the measured ε is lower at pH 7.0. This is probably due to fast adsorption, leading to the formation of inhomogeneous film structures. In fact, compared with pHs above the isoelectric point (pI4.3), acidic conditions slow down the adsorption, but the modulus is increased. Pea-protein-stabilized emulsions are more stable to creaming at acidic pH and their particle-size distributions are more homogeneous in these conditions. Effect of pH on interfacial properties and on properties of oil-in-water emulsions stabilized by PPI was interpreted in terms of pea protein solubility, globulin dissociation, and oil-droplet surface electrostatic charge. We propose that at acidic conditions, adsorbed dissociated globulins form stronger and denser viscoelastic networks when adsorbed at oil-water interface. Consequently, the pH-dependence of pea-globulin-stabilized emulsions properties could be of great interest to tune barrier properties of oil/water interfacial membranes for several applications such as encapsulation and controlled release of lipophilic bioactive components within the food, medical, and pharmaceutical industries.

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“…After mixing and pasteurization (80°C during 30 s), 0.8w/w% NaCl was added. To prevent bacterial growth, 0.2w/w% sodium azide was added to the mixture as previously done by Cases et al (2005). Rennetting was done with addition of 25 lL of rennet for 1 L of preparation (''Chymax plus'', Chr Hansen, France).…”

Section: Processed Cheesementioning

confidence: 99%