Primary proteolysis of white brined goat cheese monitored by high molarity Tris buffer SDS- PAGE system

Abstract

The aim of this work was to investigate primary proteolysis of white brined goat cheese prepared from raw milk and to correlate with the results obtained with high-molarity Tris buffer electrophoretic system. Proteolytic changes of white brined cheese were monitored by three parameters, the total protein, the water soluble proteins and the degree of proteolysis, whereas the change of major casein fractions was followed by electrophoresis in reducing conditions. Ripening caused a decrease of the total protein content, whereas in the first forty days the water soluble protein and the degree of proteolysis increased. Both casein fractions (alpha(s)- and beta-casein) of goat cheese were susceptible to primary proteolysis but to the different extent. alpha(s1)-casein disappeared during processing, whereas during 60-days of ripening the content of alpha(s2) and beta-casein was reduced by 38.90 %, and 30.72 %, respectively. Such trends of major casein fractions were strongly correlated with the degree of proteolysis and the moisture content, whereas no correlation was found between them and the water soluble protein content. The results of our investigation clearly suggested that SDS-PAGE method based on high-molarity Tris-buffer system could be a very useful for purposes of monitoring the white goat cheese proteolysis.