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Journal of Dairy Science Vol. 47 No. 10 1052-1055
© 1964 by American Dairy Science Association ®
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Photooxidation of ß-casein

C. A. Zittle, E. B. Kalan, M. Walter and T. M. King

Eastern Regional Research Laboratory,1 Philadelphia, Pennsylvania

ABSTRACT

ß-Casein was readily photooxidized at pH 8.6 and 37 C with the reduction or disappearance of histidine, tryptophan, and tyrosine, in the order given. ß-Casein oxidized to the extent of 18 moles of O2 per 30,000 g casein was no longer precipitated by calcium chloride. The binding of calcium ions to ß-casein was changed little or none by photooxidation. Photooxidation led to changes in ultraviolet absorption and a reduction in electrophoretic mobility in starch-gel-urea.


FOOTNOTES

1 Eastern Utilization Research and Development Division, Agricultural Research Service, USDA.







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