Biomedical subjects

S Marchesseau

Publications and source records attributed to S Marchesseau.

3 recordsLinked to original sources

PubMed2004

Rennet-induced gelation of calcium and phosphate supplemented skim milk subjected to CO2 treatment.

A Doehlert design was performed to study the effect of calcium and phosphate supplementation at 0 to 25 mmol/kg and 0 to 16 mmol/kg, respectively, on the rennet gelation of reconstituted skim milk subjected to pH-reversible CO(2) acidification. Supplemented reconstituted skim milk samples were acidified to pH 5.80 by the addition of CO(2) under pressure and depressurized under vacuum to restore the initial pH value. The second-order polynomial models satisfactorily predicted the effect of salt addition on the micellar molar Ca:P ratio and the average diameter of the casein micelles, whereas only trends were used in the analysis of the rennet-clotting behavior of salt-supplemented, CO(2)-treated milk. Whether added Ca was the most determinant factor on the micellar molar Ca:P ratio, added Pi (a mixture of Na(2)HPO(4) and NaH(2)PO(4)) was the most determinant factor on the other responses studied, and its effect was most pronounced when Ca was simultaneously added. By comparison with control samples, changes observed in this study were essentially due to salt supplementation and not to the CO(2) treatment. Therefore, this CO(2) treatment could be considered as an entirely reversible treatment rather than only pH-reversible, and predictions might be applied to untreated milk. In the case of Ca-supplemented milk, the micellar molar Ca:P ratio increased, the average micellar diameter decreased, and the rennet-clotting properties were improved, whereas opposite effects were observed upon Pi supplementation. Since modification of the micellar molar ratio is the result of change in the chemical composition of micellar calcium phosphate, the effect of calcium and phosphate supplementation on the rennet clotting of milk was found to be also dependent on the nature of the interaction between caseins and colloidal calcium phosphate.

Animals↗

PubMed2002

Effect of salt addition on the micellar composition of milk subjected to pH reversible CO2 acidification.

Response surface methodology was used to investigate the effect of salt supplementation on the micellar composition of reconstituted skim milk subjected to acidification by CO2 pressure to pH 5.8, followed by depressurization under vacuum. Using a Doehlert design, calcium and phosphate were added to skim milk in the range of 0 to 25 mmol/kg and 0 to 16 mmol/kg of milk, respectively, and the pH was adjusted to 6.65 +/- 0.02. After carbonation, the milk sample was depressurized, and the pH returned to its initial value without modification of the ionic strength. Micellar composition was assessed by the concentration of micellar Ca, P, Mg, and protein, and the buffering properties of milk. The second order polynomial models satisfactorily predicted the effect of salt supplementation on the micellar composition (R2adj > 0.75). Added calcium was the most determinant factor, and favored the removal of Ca, P, Mg, and proteins from the soluble phase to the micellar phase when this addition was less than 17.5 mmol/kg of milk. Above this concentration, only the concentration of micellar Ca increased. The buffering response surface showed that the amount of micellar calcium phosphate increased to a maximum upon addition of 17.5 mmol of Ca/kg. By comparison with a control sample (supplemented but untreated skim milk), changes were essentially due to salt supplementation and not to the CO2 treatment. We suggest that Ca formed micellar calcium phosphate when added at a concentration less than 17.5 mmol/kg; whereas above this concentration, Ca bound directly to micellar proteins.

Animals↗

PubMed2002

Casein interactions studied by the surface plasmon resonance technique.

Surface plasmon resonance technique was investigated for the first time to study the apparent hydrophobicity and association properties of the major bovine caseins: alpha(s)-(alpha(s1)- and alpha(s2)-caseins in a 4:1 proportion), beta-, and kappa-caseins. The apparent hydrophobicities of the caseins were evaluated by a new method based on the binding level of casein on a hydrophobic sensor chip, and kinetic and equilibrium affinity constants were determined for the following casein interactions: alpha(s)/alpha(s), alpha(s)/beta, alpha(s)/kappa, beta/beta, and beta/kappa, using a sensor chip modified with covalent immobilized caseins. The study by surface plasmon resonance technology of these casein interactions under different conditions (pH, ionic strength, calcium concentration, chemical modification) demonstrated that, at neutral pH, electrostatic repulsive forces play an important role since an increase in ionic strength of the medium resulted in a stronger interaction. When charge repulsions were reduced by either acidification, increase in ionic strength, or dephosphorylation, casein interactions were reinforced, presumably due to weak attractive forces. Moreover, in this molecular model, we showed that addition of calcium greatly increased the binding response between the most phosphorylated caseins and that the added calcium (2 mM) participated directly in the formation of bridges between the phosphate groups of the casein molecules.

Adsorption↗