Ultrasound effects on the assembly of casein micelles in reconstituted skim milk.

Reconstituted skim milks (10 % w/w total solids, pH 6·7-8·0) were ultrasonicated (20, 400 or 1600 kHz at a specific energy input of 286 kJ/kg) at a bulk milk temperature of <30 °C. Application of ultrasound to milk at different pH altered the assembly of the casein micelle in milk, with greater effects at higher pH and lower frequency. Low frequency ultrasound caused greater disruption of casein micelles causing release of protein from the micellar to the serum phase than high frequency. The released protein re-associated to form aggregates of smaller size but with surface charge similar to the casein micelles in the original milk. Ultrasound may be used as a physical intervention to alter the size of the micelles and the partitioning of caseins between the micellar and serum phases in milk. The altered protein equilibria induced by ultrasound treatment may have potential for the development of milk with novel functionality.

Ultrasound improves the renneting properties of milk.

The effects of ultrasound application on skim milk (10% w/w total solids at natural pH 6.7 or alkali-adjusted to pH 8.0) prior to the renneting of milk at pH 6.7 were examined. Skim milk, made by reconstituting skim milk powder, was sonicated at 20kHz and 30°C (dissipated power density 286kJkg(-1)) in an ultrasonic reactor. The rennet gelation time, curd firming rate, curd firmness, and the connectivity of the rennet gel network were improved significantly in rennet gels made from milk ultrasonicated at pH 8.0 and re-adjusted back to pH 6.7 compared to those made from milk sonicated at pH 6.7. These renneting properties were also improved in milk sonicated at pH 6.7 compared to those of the non-sonicated control milk. The improvements in renneting behavior were related to ultrasound-induced changes to the proteins in the milk. This study showed that ultrasonication has potential to be used as an intervention to manipulate the renneting properties of milk for more efficient manufacturing of cheese.

Effect of the ionic strength of pulsed electric field treatment medium on the physicochemical and structural characteristics of lactoferrin.

Pulsed electric field (PEF) treatment (35 kV cm(-1) for 19.2 µs using bipolar 2 µs pulses) was conducted on bovine lactoferrin (LF; 0.4 mg mL(-1)) prepared in simulated milk ultrafiltrate (SMUF), at concentrations between 0.2× and 2× normal strength, with electrical conductivities ranging from 0.17 to 1.04 S m(-1). The physicochemical and structural characteristics (LF content by a spectrophotometric and an ELISA method, surface hydrophobicity, electrophoretic mobility, far-UV circular dichroism spectra, and tryptophan fluorescence) of LF dissolved in SMUF of all strengths tested were not changed after PEF treatment. The PEF treatment of LF in 0.2 strength SMUF did not cause the release of LF-bound ferric ion into the aqueous phase, with a concentration of LF-bound iron being the same as that of the untreated LF control (174 µg L(-1)). However, in treatment media with higher ionic strengths, ferric ion was released from the LF molecule into the aqueous phase. The concentration of LF-bound iron decreased from 174 µg L(-1) for the LF treated in 0.2 strength SMUF to 80 µg L(-1) for that treated in double-strength SMUF. The results suggest that the PEF-induced iron depletion of LF does not appear to cause an appreciable conformational change in LF molecules. PEF treatment could be developed as a novel physical way to produce iron-depleted LF, as an alternative to the existing chemical method.