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Department of Food Science, University of Illinois, Urbana 61801
ABSTRACT
Brine soluble proteins of Cheddar and Gouda cheese prepared from milks of different composition were characterized by origin, composition, and electro-phoretic properties. The protein originated in the cheese curd, but its composition was not constant throughout aging. Initially,
s1-casein and ß-casein were the major electrophoretic components, but 5 h after addition of rennet extract two hydrolytic components appeared. In both varieties, the
s1-casein decreased with the production of additional components. Change was less in the ß-casein component.
Although the electrophoretic patterns of the cheeses were much less distinct than those of the corresponding brine soluble proteins, the number of components was the same in each case.
Enrichment of milk with calcium and variety characteristics (i.e., Cheddar or Gouda) had a greater influence on the electrophoretic properties of brine soluble proteins than did the casein/fat ratio of the milk.
s1-casein tended to be hydrolyzed more rapidly in Gouda than in Cheddar cheese.
1 Data from a thesis submitted to the graduate college, University of Illinois, for partial fulfillment of requirements for the Ph.D. degree, 1972. Present address: Dairy Technologist, Nat'l Dairy Research Institute, Karnal, Haryana, India.
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