Influence of pH on proteolysis in water solutions of milk protein concentrate and composition of rennet gels
2002
Zbikowska, A. | Szerszunowicz, I. (University of Warmia and Mazury, Olsztyn (Poland). Inst. of Food Biotechnology)
It was found that the stability of colloidal protein system at pH 6.6 and 6.0 as measured by the amount of chymosin-released peptides in the point of visually observable aggregation, was lower compared with that of milk. A decreased role of Ca in the formation of gel at pH 6.0 did not have the influence on the content of nitrogen in the matrix of gels. It was observed a small decrease in the relative percentage of casein in the proteins forming the matrix at pH 6.0. At the same time, it was found a decreased percentage of beta-lactoglobulin in the soluble fraction of gels. A significant decrease in the Ca/N w/w ratio in the gel matrix at pH 6.0 indicated an increased role of hydrophobic interactions in the formation
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