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   <subfield code="a">Formation and stabilization of emulsion with A1, A2 and B β-casein genetic variants</subfield>
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   <subfield code="c">[Małgorzata Darewicz, Jerzy Dziuba]</subfield>
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   <subfield code="a">The milk protein β-casein (β-CN) is a flexible, approximately random coil protein with a molecular mass of ∼24kDa. It contains distinct charged and hydrophobic, non-charged regions in the primary structure. The strongly amphiphilic nature of β-casein causes it to concentrate at an interface, which is a prerequisite to form and stabilize emulsions. The emulsifying (particle-size distribution, turbidity measurement) and structural (surface coverage, CD) properties of β-casein genetic variants were studied at pH 6.7 and I=75mM (representative pH value for milk). β-Casein B variant produced bigger emulsion droplets than the A1 and A2 variant, having better emulsion-stabilizing properties than A2 and A1 variants. Significant differences were observed in the surface coverage of teflon droplets made with β-casein genetic variants. A relationship between the surface load and emulsion-stabilizing properties was found. An increased content of secondary structure, especially for β-CN B and A1 variants, was found after adsorption onto the hydrophobic surface.</subfield>
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