skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: The use of radiolabelled milk proteins to study thermally-induced interactions in milk systems

Thesis/Dissertation ·
OSTI ID:7255506

Heat induced complexes between milk proteins are of considerable importance in determining the heat stability and rennin clottability of milk products. Thiol-disulfide interchange reactions have been suggested as the principal reaction mechanism for complex formation. Studies to data have not adequately established the mechanism and stoichiometry of complex formation in situ in total milk system. Tracer amounts of {sup 14}C-{beta}-lactoglobulin and {alpha}-lactalbumin were heated under various conditions. After clotting with rennet, radioactivity retained in the curd was counted to estimate extent of interaction of {beta}-lactoglobulin with casein. {sup 14}C- and {sup 3}H-Methyl labelled proteins were used for the preparation of radiolabelled artificial casein micelles. These micelles with radiolabelled whey proteins were heated and heat-induced complexes were separated on Sephacryl S-300 eluting with 6 M guanidine hydrochloride to break all non-covalent bonds. Further separation of the protein complexes was obtained using CPG-10 or Sephacryl S-1000. The ratios of {sup 3}H to {sup 14}C labelled proteins in the protein complexes suggested that the stoichiometries of k-, {alpha}{sub s2}-casein, {beta}-lactoglobulin and {alpha}-lactalbumin in the heat-induced complexes varied as a function of the heat treatment.

Research Organization:
California Univ., Davis, CA (USA)
OSTI ID:
7255506
Resource Relation:
Other Information: Thesis (Ph. D.)
Country of Publication:
United States
Language:
English