Abstract
Two samples of highly purified bovine beta-casein supplied to us by Dr. T.A.J. Payens of the National Institute for Dairy Research, Ede, The Netherlands, were studied over a range of concentration from just below the critical micelle concentration (CMC) to 0.46%, in 0.2 ionic strength phosphate buffer (pH 7.0), at 20 and 25 degrees C. The relaxation process studied by pressure jump using a 90 degree scattered light detector was also confirmed by the temperature-jump method. In the pressure-jump experiments, the process could be separated into two general time domains, with an approximate ratio of 10-25:1, a behavior reminiscent of that found for synthetic micellar systems. The faster relaxation process was still exhibited below the CMC, however. The concentration dependence of the faster relaxation time agreed very satisfactorily with predictions from the micelle model described in the companion paper.
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