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Surface Hydrophobicity of Physicochemically and Enzymatically Treated Milk Proteins in Relation to Techno-functional Properties
60
Citations
45
References
2007
Year
Food ChemistryProtein ChemistryEngineeringBiochemistryProtein FoldingFood AnalysisFood BiophysicsBiotechnologySurface HydrophobicitySh ValuesFoam FormationProtein Phase SeparationProtein RefoldingTechno-functional PropertiesFood TechnologyBiomolecular EngineeringHealth Sciences
Surface hydrophobicity (SH) of milk proteins treated physicochemically (by heating and Maillard reaction) or modified enzymatically (by transglutaminase, lactoperoxidase, laccase, and glucose oxidase) was assessed in relation to their techno-functional properties. Heat-treatment increased SH of whey protein isolate and decreased SH of sodium caseinate and bovine serum albumin. Maillard reaction of milk proteins caused time-depended decreases of SH. Only for total milk protein reacting with glucose and lactose elevated SH-values were detected. Protein modification with transglutaminase, laccase, and lactoperoxidase strongly increased the SH of whey protein isolate and total milk protein. Incubation with glucose oxidase elevated SH values of sodium caseinate, whey protein isolate, and total milk protein. When correlating SH with techno-functional properties, a positive correlation was observed between SH and foam formation, and a negative correlation was observed between SH and foam stability as well as emulsion stability. No clear correlation was detected between SH and emulsifying activity, surface tension, viscosity, and heat stability of enzymatically and physicochemically treated milk proteins.
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