Browning and fluorescence development during microwave irradiation of a lysine/(E)-4,5-epoxy-(E)-2-heptenal model system

Zamora, Rosario; Hidalgo, Francisco

doi:10.1021/jf00023a043

Cited by 14 publications

(16 citation statements)

References 8 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…These 1-substituted 2-(l'-hydroxypropyl)pyrroles polymerized spontaneously in solution via a reaction that was characterized (20), and the polymers produced exhibited color and fluorescence analogous to the melanoidins isolated from sugar/amino acid reactions. This similarity in color and fluorescence, produced in both oxidized lipid/amino acid and sugar/amino acid reactions, also was observed when both systems were irradiated in a microwave oven (21). In a search for new natural antioxidants, the objective of the present study was to investigate the antioxidative activity of the compounds characterized in the EH/lysine system.…”

mentioning

confidence: 62%

Natural antioxidants produced in oxidized lipid/amino acid browning reactions

Alaiz

Zamora

Hidalgo

1995

J Americ Oil Chem Soc

Self Cite

View full text Add to dashboard Cite

1-Substituted pyrroles (1 and 2) and 1-substituted 2-(l'-hydroxypropyl)pyrroles (3)(4)(5) were produced in reactions between a lipid peroxidation product, 4,5(E)-epoxy-2(E)-heptenal, and the amino acid lysine. The antioxidative activity of compounds 1-5 was studied. Oxidative stability was evaluated in refined soybean oil containing compounds 1-5, buty[ated hydroxytoluene (BHT), n-propyl gallate or L-lysine, at concentrations of 50-200 ppm. Oils were either oxidized at 60°C and oxidation products determined by the thiobarbituric acid-reactive substances assay, or they were oxidized at 110°C by the Rancimat method. Although both methods gave similar results, greater differences were observed at 60°C than at 110°C. Addition of compounds 1-5, L-lysine, BHT, and propyl gaiiate significantly (P < 0.01) protected the oil against oxidation. The effectiveness order found was: L-lysine << compounds 3-4 < compounds 1-2 < compound 5 = BHT << propy [ gallate. JAOCS 72, 1571[ gallate. JAOCS 72, -1575[ gallate. JAOCS 72, (1995.

show abstract

mentioning

confidence: 62%

Natural antioxidants produced in oxidized lipid/amino acid browning reactions

Alaiz

Zamora

Hidalgo

1995

J Americ Oil Chem Soc

Self Cite

View full text Add to dashboard Cite

show abstract

“…There are no -SH groups in mammalian myoglobins (Livingston and Brown, 1981) and thus their hypothesis would not explain our results. Secondary lipid oxidation products have been reported to interact with histidine (Alaiz and Giron, 1994;Tsai and Sokoloski, 1995); or amine groups of amino acids, including lysine via Schiff's base formation (Hidalgo and Zamora, 1993;Zamora and Hidalgo, 1992). Such formation between secondary lipid oxidation products with histidine or amine groups of oxymyoglobin may cause a conformational change in the protein.…”

Section: Resultsmentioning

confidence: 99%

Oxymyoglobin Oxidation as Affected by Oxidation Products of Phosphatidylcholine Liposomes

Chan

Faustman

Decker

1997

Journal of Food Science

View full text Add to dashboard Cite

Supernatants (105,000 ϫ g) of oxidized phosphatidylcholine (PC) liposomes contained higher levels of thiobarbituric acid-reactive substances, and caused greater metmyoglobin formation when combined with oxymyoglobin than those of controls (C) or PC plus tocopherol (PCT) (PϽ0.05). Products of PC liposome oxidation crossed dialysis membranes (mol wt cut-off ϭ 500 Dalton) and accelerated the oxidation of oxymyoglobin more than C or PCT (PϽ0.05). The addition of known oxidation products of oleic acid and linoleic acid, fatty acids typical of PC, accelerated oxymyoglobin oxidation relative to controls (PϽ0.05). Results demonstrated that oxidation products of PC were prooxidative towards oxymyoglobin.

show abstract

“…(E)-4,5-Epoxy-(E)-2-heptenal (EH) was selected as the model lipid peroxidation product because of its high reactivity with free amino groups in amino acids and proteins (Zamora and Hidalgo, 1992; and because the mechanisms involved in these reactions are now well-known Zamora and Hidalgo, 1994).…”

Section: Introductionmentioning

confidence: 99%

Antioxidative Activity of Nonenzymatically Browned Proteins Produced in Oxidized Lipid/Protein Reactions

Alaiz

Hidalgo

Zamora

1997

J. Agric. Food Chem.

Self Cite

View full text Add to dashboard Cite

The antioxidative activity of nonenzymatically browned proteins was studied to analyze the contribution of oxidized lipid/amino acid reaction products (OLAARP) to the antioxidative activities observed for proteins and protein hydrolysates. Bovine serum albumin (BSA) was incubated overnight with (E)-4,5-epoxy-(E)-2-heptenal at 37°C and later fractionated on Sephacryl S-200-HR. Two modified protein fractions were obtained, which corresponded to monomeric and dimeric modified BSA (MBSA and DBSA, respectively). Both MBSA and DBSA exhibited decreased basic amino acid residues and the presence of OLAARP residue -N-pyrrolylnorleucine. BSA, MBSA, DBSA, and butylated hydroxytoluene (BHT) (added at 10, 30, and 50 ppm) were tested for antioxidative activity in soybean oil using the thiobarbituric acid-reactive substances (TBARS) assay, and all of them significantly (p < 0.05) decreased TBARS formation. The order of effectiveness obtained was BSA < MBSA < DBSA < BHT and was parallel to the number of OLAARP residues in the protein. These results suggest that OLAARP formation conferred to the modified protein their antioxidative activities.

show abstract

Browning and fluorescence development during microwave irradiation of a lysine/(E)-4,5-epoxy-(E)-2-heptenal model system

Cited by 14 publications

References 8 publications

Natural antioxidants produced in oxidized lipid/amino acid browning reactions

Natural antioxidants produced in oxidized lipid/amino acid browning reactions

Oxymyoglobin Oxidation as Affected by Oxidation Products of Phosphatidylcholine Liposomes

Antioxidative Activity of Nonenzymatically Browned Proteins Produced in Oxidized Lipid/Protein Reactions

Contact Info

Product

Resources

About