Effect of glucose-lysine Maillard reaction product fractions on tissue xenobiotic enzyme systems

• Published in: Journal of agricultural and food chemistry Vol. 41; no. 12; pp. 2359 - 2363
• Main Authors: Kitts, David D, Wu, Chiu H, Powrie, William D
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 01.12.1993
• Subjects: ACTIVIDAD ENZIMATICA; ACTIVITE ENZYMATIQUE; Biological and medical sciences; CITOCHROMO B; CYTOCHROME B; FOIE; Food industries; Fundamental and applied biological sciences. Psychology; General aspects; GLICOSILTRANSFERASAS; GLUCOSA; GLUCOSE; GLYCOSYLTRANSFERASE; HIGADO; INGESTION DE ALIMENTOS; INTESTIN; INTESTINOS; LISINA; LYSINE; METALLOPROTEINE; METALPROTEINAS; Methods of analysis, processing and quality control, regulation, standards; OXIDORREDUCTASAS; OXYDOREDUCTASE; POUMON; PRISE ALIMENTAIRE (HOMME); PULMONES; RATON; REACCION DE MAILLARD; REACTION DE MAILLARD; REIN; RINONES; SOURIS; TOXICIDAD POR INGESTION; TOXICITE PAR INGESTION; TRANSFERASAS; TRANSFERASE; XENOBIOTICAS; XENOBIOTIQUE; Benzopyrene; Diet; Animal feeding; Lysine; Toxicity; Reaction product; Enzymatic digestion; Maillard reaction; Molecular interaction; Glucose; Polycyclic aromatic compound; Xenobiotic
• ISSN: 0021-8561; 1520-5118
• DOI: 10.1021/jf00036a027

Maillard reaction product (MRP) fractions were prepared from a glucose-lysine (gluc-lys) browning model system by heating 1.0 M solutions of glucose and lysine at 121 degrees C 4 h. MRP systems were fractionated into a melanoidin precipitate and a supernatant by the addition of absolute ethanol to a level of 90% volume. The fractions were freeze-dried and called freeze-dried supernatant (FDS) and freeze-dried melanoidin precipitate (FDMP). Chronic animal feeding studies were conducted with the addition of FDS and FDMP to experimental synthetic diets at a 2% level in mice, either B[a]P treated or untreated. At 10 weeks, animals were sacrificed and specific xenobiotic metabolizing enzymes [aryl hydrocarbon hydroxylase (AHH), glutathione S-transferase (GST), cytochrome b5, cytochrome P-450, and UDP glucuronyltransferase (UDPGT)] in the liver, lung, kidney, and small intestine microsomes and cytosol samples were measured. There was no adverse effect of the presence of MRP fractions in the diet on body growth of the mice or on the liver, kidney, lung, and intestine weights. Hepatic, kidney, and pulmonary xenobiotic enzyme activities were unchanged in mice fed both MRP fractions. Both FDS and FDMP fractions were found to significantly (P 0.05) reduce the activities of AHH and UDPGT in the small intestine mucosa of mice. In B[a]P-treated animals, AHH enzyme activities were increased in hepatic, pulmonary, and kidney tissues. FDS and FDMP fractions had no effect in modifying the enzyme activities in these animals. There were similar increases in AHH and UDPGT activities in the small intestinal mucosa of b[a]P-treated animals on FDS and FDMP diets. Our results indicate that the effect of both FDS and FDMP fractions on tissue xenobiotic metabolizing enzymes studied herein was limited to the small intestine