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Effect of stirring on the secondary structure of amyloid fibrillogenesis of β-lactoglobulin (βLG) at pH 2 and at pH 7 with and without glucose was studied. Fibrillogenesis at pH 2 was carried out by heating the 4w % β-lactoglobulin and at pH 7 by heating the 0.30 mM β-lactoglobulin in 0.1 M, pH 7 sodium phosphate buffer solution with and without glucose (37.5 mM) for 24 h under stirring (250 and 474 rpm) conditions. For control samples, β-lactoglobulin solutions were incubated under unstirred condition at pH 2 and pH 7. The secondary structure of the amyloid fibrils which corresponds the β-sheet structure was studied by using Fourier transform infrared (FTIR) spectroscopy revealed that the stirring does not affect the secondary structure of the β-lactoglobulin fibrils at pH 2 as well as pH 7 with and without glucose.

By means of a small heating coil, the temperature of a thermocouple junction is made to oscillate regularly between two temperatures T1 and T2. Simultaneously the junction makes about one contact every two seconds with the surface being measured. A short-period galvanometer in the thermocouple circuit produces on a moving photographic film a serrated sine curve whose serrations vanish once for every half-oscillation at a point that corresponds to the surface temperature T3, provided T3 lies between T1 and T2. This mode of measurement minimizes disturbances due to air currents. Alternatively, use of a thermocouple with two adjacent junctions is proposed. A simple but accurate portable thermostat for maintaining reference junctions temperatures somewhat higher than room temperature is also described.

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