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Soymilk was prepared by ohmic heating. Heating time decreased as the applied voltage was increased. Precipitation, viscosity and surface hydrophobicity of protein in the soymilk were increased with the decrease in voltage applied. Voltages of 50 and 100 V resulted in a higher heating rate and consequent formation of a larger amount of protein particles (soluble aggregates), ranging from 40 to 120 nm in size, than the other conditions. Furthermore, soymilk prepared by ohmic heating at 50 or 100 V was converted into firmer tofu curd than that at 30 V. Ohmic heating at 30 V was thought to form larger protein particles than that at 50 and 100 V, and the resultant larger sized aggregates are considered to result in inferior tofu curd texture. [ABSTRACT FROM AUTHOR]

Many radionuclides were scattered by the explosion at the Fukushima Daiichi Nuclear Power Station. We examined whether lactic acid bacteria (LAB) can sorb cesium ions (Cs+) and strontium ions (Sr2+) for radioprotection. Many strains showed biosorption to Cs+ and Sr2+ using an in vitro mass-screening although each strain showed different sorption. We selected MYU 111, MYU 758, and MYU 759 strains that showed especially high biosorption to Cs+ and/or Sr2+. MYU 111 was identified as Lactobacillus plantarum, and MYU 758 and 759 were Pediococcus pentosaceus. The selected strains tended to show higher biosorption when using the buffer method compared to the culture method. Further, they showed high biosorption at a low concentration of 1 ppb Cs+ and Sr2+ (max 28.8% and 97.7% sorption, respectively). This is the first study where lactic acid bacteria are shown to have biosorption of Cs+ and Sr2+. [ABSTRACT FROM AUTHOR]

Soybeans and the processed food, soybean milk, have important health functions. A cheese-like food produced from soybean milk resembles casein protein in its mouthfeel and physical properties. The intracellular soybean milk curdling enzyme-producing Saccharomyces bayanus SCY003 strain was screened. The curdling enzyme is an intracellular protease, a 45 kDa monomer protein that degrades soy protein subunits, produced by this strain. The optimum temperature and pH of enzyme activity are 50°C and pH 7.5, respectively. The protease degrades P-conglycinin and parts of glyeinin in soy protein to α, α and β subunits. The rheological characteristics of the resultant curd were assessed, and revealed that elasticity differed from curd produced by glucono δ-lactone, which is used in tofu production. A new soy protein food having health-supporting functions will be developed using this protease. [ABSTRACT FROM AUTHOR]