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1.
J Food Sci Technol ; 56(12): 5309-5316, 2019 Dec.
Article in English | MEDLINE | ID: mdl-31749478

ABSTRACT

In this study, thermosonication was used as a combined treatment of raw goat milk (RGM) using pasteurization (72 °C for 15 s) and ultrasound treatments (20 kHz at the power variance of 150 W, 200 W, 300 W and 400 W for 10 min). Investigation on the impact of the microbial load, protein content, protein aggregation, the particle size of fat and casein micelles, pH, viscosity, turbidity, color, and soluble calcium and phosphorus contents were carried out, whiles RGM and PGM served as the control. Our results revealed that at 400 W, that thermosonication resulted in a significant reduction (α = 0.05) in the microbial load of the samples to less than 2.3 log cfu/mL in comparison to those of RGM and pasteurized goat milk (PGM) at 5.94 log cfu/mL and 4.76 log cfu/mL respectively. In RGM, the fat size (3.5 µm) decreased to 0.4 µm at 300 W; while those of casein micelles also decreased from 406 to 256.4 nm at 400 W. However, no significant effect was observed in the color and soluble calcium and phosphorus contents of all samples. The effect on the microbial load and fat homogenization would promote thermosonication process in the dairy industry.

2.
J Dairy Sci ; 101(6): 4879-4890, 2018 Jun.
Article in English | MEDLINE | ID: mdl-29573795

ABSTRACT

Gamma radiation has been used in food processing for many years, though it has certain effects on food components. Whey protein solutions (10%/30%, wt/vol) were treated with gamma radiation at various dosages (10-25 kGy) and evaluated for microbial changes in the solutions and physicochemical and structural changes of whey proteins. Whey protein solutions after gamma radiation showed substantially lower populations of all viable microorganisms than those of controls. The 10% whey protein solution treated at radiation of 20 or 25 kGy remained sterile for up to 4 wk at room temperature. Gamma radiation increased viscosity and turbidity and decreased soluble nitrogen of whey protein solutions compared to nonradiated control samples regardless of radiation dosage. Nonreducing sodium dodecyl sulfate-PAGE suggested that whey proteins under gamma radiation treatment formed aggregates with high molecular weights. Reducing sodium dodecyl sulfate-PAGE showed that disulfide bonds played a role in gamma radiation-induced whey protein cross-linking. Scanning and transmission electron microscopy micrographs exhibited large aggregates of whey proteins after gamma radiation treatment. Results suggested that gamma radiation could be applied to whey protein solution for purposes of reducing microbial counts and cross-linking protein molecules.


Subject(s)
Bacteria/radiation effects , Whey Proteins/radiation effects , Whey/microbiology , Animals , Bacteria/classification , Bacteria/genetics , Bacteria/isolation & purification , Cattle , Electrophoresis, Polyacrylamide Gel , Food Irradiation , Gamma Rays , Microscopy, Electron, Transmission , Models, Biological , Viscosity , Whey/radiation effects , Whey Proteins/chemistry
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