Rosco and Fuller

Figure 5. Adsorption isotherms for proteins in phosphate buffer (pH 7.0,299 K) with an anodic end potential of 0.4 V (vs. SCE) , )9-lactoglobulin A a, lysozyme , ribonuclease A. (Reprinted from Roscoe and Fuller, with permission.)...

Heat affects the conformation of proteins, and most proteins undergo fairly rapid heat denaturation somewhere between 333 and 363 A series of experiments was made by Roscoe and Fuller in which the surface adsorption behavior of bovine )8-lactoglobulin A, hen egg-white lysozyme and bovine pancreatic ribonuclease A was studied at a platinum electrode as a function of temperature using cyclic voltammetry. The protein solution and the electrochemical cell were separately immersed in the thermostated bath and allowed to equilibrate for 30 mins. The protein... 

Figure 24. Surface charge density,of protein at a platinum electrode versus the time of potential sweeping after the electrode was dipped in protein solution(s) in phosphate buffer (pH 7.0,368 K) and measured at 273 K. , dipped in a /c-casein solution (0.13 g r ) A, dipped first in the K-casein solution and then in a -lactoglobulin solution (0.16 g 1" 2 min dip each v, dipped first in the /c-casein solution followed by the jff-lactoglobulin solution, 8 min dip each , dipped first in the )ff-lactoglobulin solution followed by the /c-casein solution, 2 min dip each O, dipped first in the J -lactoglobulin solution followed by the /c-casein solution, 8 min dip each. (Reprinted from Roscoe and Fuller with permission.)...

L. Fuller and S. G. Roscoe, in Protein Structure-Function Relationships in Foods, Ed. by R. Y. Yada, R. L. Jackman, and J. L. Smith, Blackie Academic and Professional Publishers, Glasgow, 1994, pp. 143-162. 

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