Model studies on the heating of food proteins--heat-induced oligomerisation of ribonuclease.
Commercial ribonuclease was heated at temperatures between 80 degrees C and 180 degrees C for 1--24 h. A stoichiometric oligomerisation was observed. Dimeric ribonuclease appeared after 1 h at 80 degrees C. With increasing time and/or temperature the number of oligomers formed rose at first. The highest oligomer that could be detected was the hexamer (140 degrees C, 8 and 16 h). A further increase in time and/or temperature resulted in a decrease of the number of oligomers and a rise in the polymer fraction. The importance of this reaction in the changes produced by heating food proteins and various reaction mechanisms are discussed.
D004044:Dietary Proteins / Q000032:analysis; D004589:Electrophoresis, Disc; D006358:Hot Temperature; D011108:Polymers; D011489:Protein Denaturation; D012260:Ribonucleases / Q000032:analysis*; D013997:Time Factors
D004044:Dietary Proteins; D011108:Polymers; D012260:Ribonucleases