Spectroscopy characterization of acid and rennet camel milk caseins using XRD, XPS, and SEM and effects on their emulsifying properties

Casein, the main protein in milk, is a viable source for natural emulsifiers, which are frequently utilized food emulsions. Camel milk casein powders obtained by acid and rennet coagulation were investigated characterized using X-ray diffraction (XRD), photoelectron spectroscopy (XPS) scanning electron microscopy (SEM). These methods gave extensive information regarding crystal structure, surface composition, secondary microstructures of camel caseins, respectively. Therefrom new acknowledgements on morphology composition have emerged, necessary to better understand functional characteristics such as emulsifying behaviour (i.e., emulsion’s stability over time oil droplet size). The O C atomic proportions surfaces generated acidification greater than those through rennet-induced coagulation, whereas percentage N was lower, according XPS measurements. oxygen carbon (O/C) ratios caseins produced two techniques comparable. But, enzymatic method yielded high (N/C) ratio. ‎The findings suggested that might influence C, O, components caseins. Furthermore, SEM XRD data revealed aggregation affected micelle’s morphology, resulting more β-sheet smooth structures. Rennet other hand, porous colloidal surface. ‎A correlation between observed, size emulsions strongly improved method.