Lysozyme content in the fractions of egg-white
2001
Mikelsone, V. | Ozola, B. | Kaulins, U. | Kolkova, J. (Latvia Univ. of Agriculture, Jelgava (Latvia). Faculty of Food Technology. Dept. of Chemistry)
The task of the experiment was to investigate the localization of lysozyme in hen egg-white fractions and to establish its thermal stability and homogeneity. As it is well known, the egg-white can be devided into two fractions - liquid and gel. The method of the given experiment is explained and the materials used are described. The experimental results show that lysozyme activity in native egg-white fractions differs only by about 1.2% whereas after the thermal denaturation the difference reaches 25.4%. It means that lysozyme protein molecules may be different. The activity of lysozyme and its changes in the native egg-white fractions are shown in table 1.
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