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The paper estimates the effect of high-pressure homogenization (20-140 MPa) on selected whole milk properties. High-pressure homogenization did not have a clear effect on the milk acidity. However, a slight increase in viscosity and a clear decrease in milk heat stability were observed along with an increase in the applied pressure. On the basis of a microscopic analysis and the measurement of the absorbance of milk samples, an increase in the fat dispersion degree was observed along with an increase in homogenization pressure up to 100 MPa. Homogenization, especially at the pressure over 80 MPa, resulted in an increase in susceptibility of milk globules to coalescence.
The chemical composition, solubility, and dispersity of milk powders obtained from milks with the 10% and 15% additions of whey and rennet coagulation time (RCT), heat and alcohol stability of the reconstituted milk were studied. The change in the proportion between casein and whey proteins in modified milk powders was found to increase the denaturation degree of ß Mactoglobulin. With an increase of the whey addition, the heat and alcohol stability decreased, and solubility index and dispersity of modified milk powders increased. The effect of whey addition on RCT of modified milk powders was different. The correlation (r=-0.99) was found between RCT and weight ratio of calcium to casein nitrogen.
Soluble invertase from mid-milky stage grains of two wheat (Triticum aestivum L.) varieties, namely Kalyansona and PBW 343 was isolated and purified by employing ammonium sulphate precipitation, gel filtration on Sephadex G-150 and DEAE-cellulose column chromatography. Invertase from Kalyansona exhibited greater heat stability (50 °C) compared to PBW 343 (35 °C). By employing photo-oxidation and chemical modification methods, and by studying the effect of pH on Km and Vmax, the involvement of histidine, sulphydryl and α-carboxyl groups in the active site of the enzyme was indicated. The enzyme was completely inhibited by HgCl₂ and DTNB. ZnSO₄, MgSO₄, KCl, CaCl₂, EDTA and pyridoxine were strong inhibitors in PBW 343 but not in Kalyansona. The two varieties also showed differential response in respect to thermodynamic properties of the enzyme, i.e. energy of activation (Ea), enthalpy change (ΔH) and entropy change (ΔS). Overall the results suggest that genetic differences exist in soluble invertase properties of wheat grains and that the thermal adaptation of the enzyme is reflected in its altered kinetic behaviour.
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