Casein Composition of Cow's Milk of Different Chymosin Coagulation Properties

Abstract

Five good and four poor chymosincoagulating individual cow milk samples were analyzed for casein composition using hydroxyapatite chromatography and polyacrylamide gel electrophoresis to establish possible relationships between casein fractions and differences in coagulation properties.Samples exhibited wide variation in casein composition. Poor chymosincoagulating milk had higher content of γ- and degraded caseins and lower κ- and β-caseins than the good-coagulating milk. One milk sample that did not coagulate 30min after chymosin addition had low αS-casein concentration and an additional major casein fragment (not identified). A substantial peak representing unidentified minor caseins was apparent in a poorcoagulating milk sample, which coagulated early but whose coagulum did not become firm in 30min. Excluding the nonclotting sample, less variability was observed in αS-casein concentrations than in the other casein components.