Turmeric may protect cells from oxidative stress by acrylamide in-vivo

Turmeric is a perennial herb; the rhizome is the portion of the plant that is used medicinally. It is the source of the spice turmeric with characteristic yellow color. Acrylamide is found in some foods that are cooked at high temperatures. It appears to be formed as a by product of the Maillard reaction. Maillard reaction is a type of non -enzymatic browning, which involves the reaction of simple sugars [carbonyl groups] and amino acids. Only the acrylamide monomer is toxic. Present work is focused on turmeric's antioxidant activity against acrylarnide toxicity. Rats were divided into three groups [7 rats/ group]. Group A served as negative control that was fed on standard diet [commercial diet] for 11 days. Group B was fed for 11 days on standard diet containing 0.34g acrylamide / kg diet as a positive control. Group C received standard diet with turmeric [0.5%] and same concentration 0.34g acrylamide/ kg diet for 11 days as a protective group. Results revealed that kidney, brain and lung tissues were disturbed when rats were fed on acrylamide diet. Turmeric had ameliorated the antioxidant status in these organs. It is concluded that turmeric as a natural antioxidant has protected from acrylamide toxicity

Maillard's reaction in parenteral solutions supplemented with arginine

Arginine, as a basic amino acid, can alter the pH of a parenteral solution and consequently to interfere in the stability of other amino acids. The objective of this study was to analyze the chemical stability of amino acids in solutions for parenteral nutrition with arginine supplementation. Amino acids concentrations were determined using an amino acid analyzer in intervals of 12, 36, 72 hours, 7 and 28 days. Storage temperatures were -20 degrees C, 5 degrees C and 25 degrees C. A decrease was observed (p < 0.05) in the concentrations of threonine, methionine, isoleucine, leucine, proline and lysine on the 28th day of study, in the solutions kept at 25 degrees C. The side chains of threonine, methionine, isoleucine, leucine, proline and lysine have hydrophobic groups, which renders them less soluble in water when compared to amino acids that have polar side chains. The degradation of lysine was significant in the sample of parenteral nutrition supplemented with arginine, possibly due to the fact that the solution's pH was between 7.5 and 7.6, therefore facilitating the Maillard reaction between lysine and glucose.