milk proteins




Fresh skimmed milk and reconstituted micellar casein samples were subjected to cavitation, with no changes observed in the size of casein micelles, free casein content and soluble calcium concentration.




This may be related to the looser structure of casein micelles at higher pH, which promotes the action of ultrasound-induced shear forces upon disruption of reassembled casein micelles.

The effect of high intensity continuous flow cavitation (with and without heat generation) on whey proteins (α-lactalbumin [α-La] and β-lactoglobulin [β-Lg]) showed greater protein denaturation than heat alone when combined with heat (61, 70 and 75.5 °C). In addition, significant synergy between controlled cavitation and heat was observed for the denaturation of α-La and β-Lg. 

Hydrodynamic cavitation for 15 min generated the highest β-sheet and SS content, while treatment for 30 min resulted in the lowest dityrosine, carbonyl and antioxidant activity.

The obtained data suggest that hydrodynamic cavitation has the potential to enhance the antioxidant activity of β-Lg. 

Similar observations were made regarding the antioxidant activity of skim milk in a linoleate emulsion system using hemoglobin as a pro-oxidant, resulting in increased antioxidant activity of skim milk and casein fractions.

This increase in antioxidant capacity of skim milk may be related to the increase in effective casein concentration following possible ultrasound-induced disruption of the casein micelle.

Various treatments showed a progressive increase in surface hydrophobicity and reactive thiol content of pure β-Lg, while α-La protein was even more affected by cavitation with a significant increase in surface hydrophobicity.

There are many applications of cavitation for manipulating the characteristics of milk proteins. Hydrodynamic cavitation has great potential for application and can be used in continuous processes due to its pump-like design.

Different treatments showed a progressive increase in surface hydrophobicity and reactive thiol content of pure β-Lg, while α-La protein was even more affected by cavitation with a significant increase in surface hydrophobicity. 

The applications of cavitation to manipulate the characteristics of milk proteins are numerous. Hydrodynamic cavitation has great application potential and can be used in continuous processes due to its pump-like design.

the major proteins in cows milk

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