To study the importance of hydrophobic interaction on the mechanism of acid milk gel formation, milk coagulation process was monitored at 30 Њ Њ Њ Њ ЊC in presence of various levels of sodium dodecyl sulphate (SDS). As a function of the SDS concentration, acid milk coagulability was either enhanced or reduced. Main pH-induced biochemical changes were preserved despite the presence of SDS (such as pH-induced demineralization and pHinduced protein solubilization). It could be assumed that SDS-modified casein micelles ability to coagulate by lowering of pH might seem to be governed essentially by the level of SDS-induced k-casein micellar dissociation, at natural milk pH.
The addition of sodium dodecyl sulfate (SDS) during skim-milk reconstitution contributed to a modification of hydrophobic interactions and, consequently, to change in the micellar structure. SDS-induced modifications in casein micelles were investigated by biochemical measurements (soluble mineral and protein analyses, granulometric and electrokinetic potential measurements, and casein micelle solvation). SDS induced micellarcasein dissociation and caused a decrease in steric, hydration, and electrostatic repulsive forces between casein micelles and as a result altered micellar stability. Consequently, SDS-modified micelle aggregation occurred. Mineral analysis indicated that Ca, PO 4 3-and Mg partitioning between aqueous phase and curd is similar, suggesting a possible bridging mechanism via minerals and SDS molecules.
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