Thermal properties of milk fat, xanthine oxidase, caseins and whey proteins in pulsed electric field-treated bovine whole milk

•Pulsed electric field treatment did not alter fat melting temperature.•Electric field treatment induced less protein denaturation than thermal treatment.•Protein surface hydrophobicity increased with the intensity of the electric field.•Pulsed electric field treatment has lower impact on milk funct...

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Veröffentlicht in:Food chemistry 2016-09, Vol.207, p.34-42
Hauptverfasser: Sharma, Pankaj, Oey, Indrawati, Everett, David W.
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Sprache:eng
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Zusammenfassung:•Pulsed electric field treatment did not alter fat melting temperature.•Electric field treatment induced less protein denaturation than thermal treatment.•Protein surface hydrophobicity increased with the intensity of the electric field.•Pulsed electric field treatment has lower impact on milk functionality than heating. Thermodynamics of milk components (milk fat, xanthine oxidase, caseins and whey proteins) in pulsed electric field (PEF)-treated milk were compared with thermally treated milk (63°C for 30min and 73°C for 15s). PEF treatments were applied at 20 or 26kVcm−1 for 34μs with or without pre-heating of milk (55°C for 24s), using bipolar square wave pulses in a continuous mode of operation. PEF treatments did not affect the final temperatures of fat melting (Tmelting) or xanthine oxidase denaturation (Tdenaturation), whereas thermal treatments increased both the Tmelting of milk fat and the Tdenaturation for xanthine oxidase by 2–3°C. Xanthine oxidase denaturation was ∼13% less after PEF treatments compared with the thermal treatments. The enthalpy change (ΔH of denaturation) of whey proteins decreased in the treated-milk, and denaturation increased with the treatment intensity. New endothermic peaks in the calorimetric thermograms of treated milk revealed the formation of complexes due to interactions between MFGM (milk fat globule membrane) proteins and skim milk proteins. Evidence for the adsorption of complexes onto the MFGM surface was obtained from the increase in surface hydrophobicity of proteins, revealing the presence of unfolded hydrophobic regions.
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2016.03.076