The influence of thermical treatment of pig liver on the concentration of water-soluble proteins was investigated. The latter can be partly separated by preparative thin-layer chromatography and characterized by UV-spectroscopy. The initial decrease in measurable protein content as a result of the denaturation was followed by a light increase. The latter was caused by an easier accessibility of the hydrophobe protein areas and by hydrolytical splitting of the proteins. The same assessment of quality is also valid for the model protein (bovine-serum albumin). The addition of glucose causes in both cases an intensive reaction between proteins and sugars--the result is in every case an increase in browning intensity.
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