School of Science, RMIT University, Bundoora West Campus, Plenty Road, Melbourne, Vic 3083, Australia.
School of Science, RMIT University, Bundoora West Campus, Plenty Road, Melbourne, Vic 3083, Australia; Spraying Systems Co., Fluid Air, Melbourne, Australia.
Ultrason Sonochem. 2019 Nov;58:104525. doi: 10.1016/j.ultsonch.2019.03.016. Epub 2019 Mar 15.
Low-frequency sonication (20 kHz) was applied to sodium caseinate suspensions (4%, 7% and 10% protein concentrations) at pH 4.0, 4.6, 6.7 and 9.0. Particle size, zeta potential and solubility analysis were used to evaluate the physical changes of the sodium caseinate suspensions before and after the application of ultrasound. At pH 6.7 the particle size remained between 5 and 7 µm for all concentrations before and after sonication (15-400 J/mL), resulting in no significant change (p > 0.05). Similarly, sonication did not significantly (p > 0.05) affect the solubility at pH 6.7. At this pH, the initial solubility was high at 94-98% (w/w) before sonication. At pH 9.0 for 4% and 7% concentrations, suspensions became more negatively charged and the initial particle size increased to 78-82 µm. In the presence of larger suspensions, the application of ≥15 J/mL reduced the particle size to less than 2 µm. By contrast to pH 6.7, the solubility at pH 9.0 for 4% and 7% protein suspensions reached 99% before and after sonication. Viscosity was the highest (80 mPa.s at 15 sec) for a 10% protein concentration at pH 9.0. As the protein concentration of the sodium caseinate suspensions decreased from 10% to 4% at pH 9.0, the viscosity of the suspensions also decreased. However, application of low-frequency ultrasound had no effect on the viscosity of the sodium caseinate suspensions. Due to the absence of large insoluble aggregates in reconstituted sodium caseinate suspensions, the overall effect of low-frequency sonication were largely insignificant at native pH and only became evident at outlier pH values when the casein proteins associate.
低频超声(20 kHz)应用于 pH 值为 4.0、4.6、6.7 和 9.0 的干酪素酸钠悬浮液(4%、7%和 10%的蛋白质浓度)。在应用超声前后,使用粒径、Zeta 电位和溶解度分析来评估干酪素酸钠悬浮液的物理变化。在 pH 值为 6.7 时,所有浓度的干酪素酸钠悬浮液的粒径在超声前后均保持在 5-7 µm 之间(15-400 J/mL),没有显著变化(p>0.05)。同样,超声对 pH 值为 6.7 时的溶解度没有显著影响(p>0.05)。在该 pH 值下,初始溶解度在超声前高达 94-98%(w/w)。对于 4%和 7%的浓度,在 pH 值为 9.0 时,悬浮液带负电荷增加,初始粒径增大至 78-82 µm。在存在较大悬浮液的情况下,应用≥15 J/mL 将粒径减小至小于 2 µm。与 pH 值为 6.7 时相比,4%和 7%蛋白质悬浮液在超声前后的 pH 值为 9.0 时的溶解度达到 99%。在 pH 值为 9.0 时,10%蛋白质浓度的悬浮液的粘度最高(15 秒时为 80 mPa.s)。随着干酪素酸钠悬浮液的蛋白质浓度从 10%降低到 4%,悬浮液的粘度也降低。然而,低频超声对干酪素酸钠悬浮液的粘度没有影响。由于再配制的干酪素酸钠悬浮液中不存在大的不溶性聚集体,因此低频超声的整体影响在天然 pH 值下基本不显著,只有在蛋白酪蛋白聚集时,在异常 pH 值下才变得明显。