The effect of ultrasound on casein micelle integrity |
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Authors: | J Chandrapala GJO Martin B Zisu SE Kentish M Ashokkumar |
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Affiliation: | * School of Chemistry/Department of Chemical and Biomolecular Engineering, University of Melbourne, Victoria 3010, Australia;† Dairy Innovation Australia, Synedes Road, Werribee, Victoria 3030, Australia |
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Abstract: | Samples of fresh skim milk, reconstituted micellar casein, and casein powder were sonicated at 20 kHz to investigate the effect of ultrasonication. For fresh skim milk, the average size of the remaining fat globules was reduced by approximately 10 nm after 60 min of sonication; however, the size of the casein micelles was determined to be unchanged. A small increase in soluble whey protein and a corresponding decrease in viscosity also occurred within the first few minutes of sonication, which could be attributed to the breakup of casein-whey protein aggregates. No measurable changes in free casein content could be detected in ultracentrifuged skim milk samples sonicated for up to 60 min. A small, temporary decrease in pH resulted from sonication; however, no measurable change in soluble calcium concentration was observed. Therefore, casein micelles in fresh skim milk were stable during the exposure to ultrasonication. Similar results were obtained for reconstituted micellar casein, whereas larger viscosity changes were observed as whey protein content was increased. Controlled application of ultrasound can be usefully applied to reverse process-induced protein aggregation without affecting the native state of casein micelles. |
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Keywords: | ultrasonication casein micelle dynamic light scattering viscosity |
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