Investigation of the activity of enzymes participating in metabolism of xenobiotics for evaluating the quqlity of protein-containing products of microbial synthesis
1990
Vysotskii, V.G. | Martinchik, A.N. | Bondarev, G.I. | Mamaeva, E.M. | Feoktistova, A.I. | Chernov, N.N. | Peskova, E.V. | Zhminchenko, V.M.
The activity of enzymes participating in the metabolism of xenobiotics in the liver of rats fed protein products obtained by the microbial synthesis method was investigated to evaluate their quality and harmlessness. It is shown that the biomass of mycelium of the fungus pubescens effected an increase in the content of cytochrome P450, activity of benzo[a]pyrene dehydroxylase and UDP-glucuronyltransferase in microsomes and glutathione reductase in liver cytosol, but did not change the activity of other enzymes related to metabolism of glutathione. The biomass of eprin yeast (yeast cultured on ethanol as the carbon source) caused an increase of the activity of bento[a]pyrene hydroxylase, glutathione-S-aryltransferase and gamma-glutamyl-transpeptidase in the liver. Paprin did not cause substantial changes in enzymes of the metabolism of xenobiotics in the liver in comparison with casein. The results indicate the absence of a direct relation between the activity of the process of metabolism of xenobiotics and biological value of protein of the investigated products. Biologically active compounds or chemical impurities contained in the protein products apparently have a modifying effect on enzymes of the metabolism of xenobiotics. The low activity of glutathione peroxidase in liver indicates the absence of selenium in the protein products, which is not included in the culture medium of the producing organisms.
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