The effect of non-thermal hydrodynamic cavitation process on structural and function properties of casein protein

Abstract

The effect of hydrodynamic cavitation (HC) on protein functionality is an emerging area of interest in the field of non-thermal processing. The effect of HC on Casein protein's physicochemical and functional properties. HC reduced the crystallization temperature from 230.9 °C in CP1 to 223.2 °C in CP2. The initial viscosity increased significantly to 39,080 Pa s from 26,590 Pa s. HC increased the concentration of amino acids following in-vitro digestion from 145.79 ± 5.7 μg/ml to 194.58 ± 6.3 μg/ml. Trypsin inhibitory reduced up to 44 ± 0.02 % in CP3. The solubility increased from 11.21 ± 0.50 μg/ml to 25.70 ± 1.44 μg/ml in CP2. The water holding capacity of the treated sample increased from 1.73 ± 0.19 g/g in CP1 to 2.52 ± 0.0036 g/g. The oil holding capacity of the treated sample decreased from 0.85 ± 0.02 g/g to 0.67 ± 0.03 g/g.

Keywords

• Casein
• Hydrodynamic cavitation
• In-vitro digestibility
• Trypsin inhibition
• Viscosity