Analysis of proteolysis in cheese using ion-exchange and reverse phase chromatography
1994
Leaver, J. | Law, A.J.R. | Banks, J.M. | Horne, D.S. (Hannah Research Inst., Ayr, Scotland (UK)) | Calvo, M.M.
Ion-exchange fast-protein liquid chromatography (FPLC) has been used to investigate changes in the levels of the various caseins during maturation of cheeses made from pasteurized milk and those made from milk heated to higher temperatures so as to denature and incorporate whey proteins into the curd. A combination of both cation- and anion-exchange chromatography was found to be necessary in order to analyse the caseins in the water-insoluble fraction, due to the co-elution of peptides with some of the principal caseins. The changes in the casein and whey protein levels as measured chromatographically were compared with those measured by extraction and precipitation techniques and by polyacrylamide gel electrophoresis. Low-fat cheeses made from pasteurized milk and milk heated to incorporate whey proteins were also examined chromatographically. In addition to separating the water-insoluble fraction, the peptide and amino acid composition of these cheeses after 34 weeks ripening were also analysed using reverse phase high pressure liquid chromatography (HPLC). Distinct differences in the peptide patterns and the amino acid content of the two types of cheeses were observed which may explain some of the variations in their flavour characteristics.
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