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The aim of the research was to study the effect of heating (72°C/15 s, 92°C/60 s) water solutions of milk protein concentrate (pH 7.1), obtained by ultrafiltration, on the enzymatic phase during chymosin activity at 32°C at pH 7.1, 6.6 and 6.0. It was found that heating at 72°C limited the number of peptides released at pH 7.1 by 33.3%, and heating at 92°C - by 25.0%. It was affected by differences in the access of the enzyme to glycosylated K-casein. After reducing pH to 6.6, it was observed that heating both at 72°C and 92°C influenced the limitation of the number of released peptides by 13%. The level of the temperature, however, influenced significant differences in RCT which was longer by 17.0% and 34.0% in the substrates heated to 72°C and 92°C. After reducing pH to 6.0, it was found that heating at 72°C and 92°C limited the number of released peptides by 11.2%. However, significant (p=0.05) elongation of RCT (by 8%) was observed only after heating at 92°C.
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.
Amino acid sequences of chicken (Gallus gallus) meat proteins: myosin, tropomyosin, troponin, collagen and connectin taken from SWISS-PROT and EMBL databases have been analysed using "PROTEIN" computer program searching for fragments identical to bioactive peptides and for bonds susceptible to the action of endopeptidases in protein chains. Chicken meat proteins contain fragments with antihypertensive (connectin), immunomodulating (myosin, tropomyosin, collagen), antithrombotic (collagen), antibacterial (collagen), embryotoxic (collagen) activity and also neuroactive (myosin, collagen, connectin) occurring in amino acid sequences with the frequency higher than that expected from the probability of appearance of given fragments in random amino acid sequences. There is a theoretical possibility of release of bioactive fragments from chicken meat proteins by endopeptidases. Such possibility especially occurs in the case of hydrolysis by proteinase K (EC 3.4.21.14). The frequency of occurrence of bioactive fragments may be applied for quantitative comparison of value of proteins as a source of bioactive peptides, although different affinity of bioactive fragments to their receptors and different susceptibility of proteins to proteolysis should be taken into consideration.
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