Effect of heat-treated proteins on selected parameters of the biotransformation system in the rat

The intake of heat-damaged proteins from food causes various effects, like the loss of essential amino acids and a reduced protein digestibility. There is also an influence on gastrointestinal microorganisms and different digestion enzymes. Until now, very little is known about the influence of heat-treated proteins on the enzymes of the biotransformation system. In the present study, the influence of protein-bound L-lysino-D,L-alanine, N(epsilon)-fructoselysine, and N(epsilon)-carboxymethyllysine (CML) on selected enzymes of the biotransformation in liver, kidney, and intestinal mucosa of male Wistar rats was examined. The contents of cytochrome P-450 and cytochrome b(5) and the activity of NADPH-cytochrome c reductase served as indicators of phase I biotransformation. The influence on phase II biotransformation was shown by the content of glutathione and the glutathione S-transferase activity. The results showed that treatment with heat-damaged proteins mainly affected phase II biotransformation enzymes with CML, yielding the strongest effect. The activity of glutathione S-transferase in the kidney was 86% higher in animals treated with diets containing 4,930 mg.kg(-1) protein-bound CML than in animals of the control group which received a diet without any detectable CML. In addition, a higher level of glutathione was found in the kidneys of animals fed on diets containing CML. The glutathione S-transferase activity was 64% higher in the intestinal mucosa of animals fed on protein-bound N(epsilon)-fructoselysine (2,700 mg.kg(-1)). The glutathione S-transferase activity was higher (p >0.05) in the intestinal mucosa of animals fed on protein-bound L-lysino-D,L-alanine (2,582 and 12,474 mg.kg(-1)). In conclusion, ingestion of heat-treated proteins led to an activation of the enzymes of phase II biotransformation. Whether or not the released pure compounds or the degradation products of the test proteins are responsible for the altered enzyme activities remains to be evaluated.