Effect of power ultrasound pre-treatment on the physical and functional properties of reconstituted milk protein concentrate

•The ultrafiltered milk retentates were treated with PUS prior to spray drying.•We examine physical and functional properties changes of MPC for PUS pre-treatment.•The pH and conductivity of MPC reconstitution did not change significantly.•The functionality of MPC such as solubility increased for PU...

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Veröffentlicht in:Journal of food engineering 2014-03, Vol.124, p.11-18
Hauptverfasser: Yanjun, Sun, Jianhang, Chen, Shuwen, Zhang, Hongjuan, Li, Jing, Lu, Lu, Liu, Uluko, H., Yanling, Su, Wenming, Cui, Wupeng, Ge, Jiaping, Lv
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Sprache:eng
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Zusammenfassung:•The ultrafiltered milk retentates were treated with PUS prior to spray drying.•We examine physical and functional properties changes of MPC for PUS pre-treatment.•The pH and conductivity of MPC reconstitution did not change significantly.•The functionality of MPC such as solubility increased for PUS pre-treatment. This work investigated the impact of power ultrasound (PUS) pretreatment on the physical and functional properties of reconstituted milk protein concentrate (MPC) 80. Ultrafiltered/diafiltered (UF/DF) milk protein retentates were treated with PUS (12.50±0.31W and 50% amplitude) for 0.5, 1, 2, and 5min prior to spray drying. Results revealed that the particle size (D50) reduced from 28.45μm to 0.13μm after 0.5min of sonication. Solubility increased significantly from 35.78% to 88.30% after 5min of PUS pre-treatment. Moreover, the emulsifying activity index (EAI) of MPC samples increased significantly as the time of ultrasonic treatment was prolonged. Additionally, the emulsion stability index (ESI) initially increased after ultrasound treatment for 1min. Surface hydrophobicity was greatly increased with more hydrophobic groups exposed to the environment. PUS pre-treatment also promoted an increase in the storage modulus (G′) of the MPC solutions. Viscosity significantly decreased after PUS pre-treatment. This result was confirmed by the microstructure of the powder, with small particles formed and trapped in dents of large particles. However, sodium-dodecyl sulfate–polyacrylamide gel electrophoresis showed no significant change in protein molecular weight.
ISSN:0260-8774
1873-5770
DOI:10.1016/j.jfoodeng.2013.09.013