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Journal of Dairy Science Vol. 68 No. 8 1887-1892
© 1985 by American Dairy Science Association ®
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Casein Composition of Cow's Milk of Different Chymosin Coagulation Properties1

L. M. Okigbo, G. H. Richardson, R. J. Brown and C. A. Ernstrom

Department of Nutrition and Food Sciences, Utah State University, Logan 84322

ABSTRACT

Five good and four poor chymosin-coagulating 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 chymosin-coagulating milk had higher content of {gamma}- and degraded caseins and lower {kappa}- and ß-caseins than the good-coagulating milk. One milk sample that did not coagulate 30 min after chymosin addition had low {alpha}S-casein concentration and an additional major casein fragment (not identified). A substantial peak representing unidentified minor caseins was apparent in a poor-coagulating milk sample, which coagulated early but whose coagulum did not become firm in 30 min. Excluding the nonclotting sample, less variability was observed in {alpha}S-casein concentrations than in the other casein components.


FOOTNOTES

1 Contribution number 3017 of the Utah Agricultural Experiment Station. Approved by the Director.




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