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The solubility of sodium coprecipitate in water and in salt solution of the composition corresponding to simulated milk ultrafiltrate was studied at 3000, 8000, 19000 and 110000 g. The molecular state of protein determining its solubility was defined together with the contribution of Ca, Mg, P, K and Na to the formation of this state. The (Ca+Mg)/(Na+K) weight ratio in the protein aggregates insoluble in the salt solution decreased with an increase in gravity. The constant (Ca+Mg)/N weight ratio and protein composition of the protein aggregates insoluble in the salt solution in the gravity ranging from 3000 to 110000 g suggested increased contributions of hydrophobic interactions and covalent bondings in the integration of protein particles as their size increased.
The objective of this work was to determine the effect of cold storage of milk on selected functional properties of micellar casein. The cold storage of milk was found to modify the molecular state of casein, changing its functional properties. The time of enzymatic coagulation was lengthened and the amount of chymosin-released peptides increased. The modification of molecular state caused the formation of milk gels of a changed structure. The changes induced by low temperature did not reverse on balancing the protein system of milk by stabilization (22724 h) or termization (65°C/15 s).
Computer analysis was used to evaluate the values of selected fish protein sequences as sources of biologically-active peptides. Two databases were used to analyze eight fish protein sequences: UniProt and BIOPEP. The main criterion of protein value applied was the profile of the potential biological activity of a protein. Bioinformatic analysis showed that all fish protein sequences were potential sources of bioactive peptides. The largest number of peptides detected among the analyzed fish proteins indicated an ACE inhibitory effect, which is the ability to reduce blood pressure. The best potential source of bioactive peptides was b-actin from European perch (Perea fluviatilis), while the smallest number of bioactive peptides were detected in a fragment of b-actin from freshwater whitefish (Coregonus lavaretus).
The conversion of muscle into meat is a complex process in which all mechanisms responsible for the development of meat qualities are very likely interdependent. Understanding the complicated biochemical mechanisms regulating cell death processes after slaughter may help us in the future to provide better solutions for pre-slaughter animal handling and post-slaughter interventions to manage meat toughness. Differentiating muscle cell death processes after slaughter from apoptosis or necrosis may consequently lead to enhanced technological meat quality. Many results have indicated that a number of molecules such as those from the caspase family are likely to be involved in the cell death process after slaughter and also in meat tenderization. Apoptosis as a unique possible route for cells and tissues of a dead animal and for all animal species may constitute a new way of thinking about the post-mortem development of the organoleptic qualities of the final product, namely meat. Analysis of the consequences of apoptosis can brings possible answers to many questions about the conversion of muscle into meat.
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