2-nonenal--(trans)-isomer and nonanal

Nonanal, (E)-2-nonenal, (E,E)-2,4-nonadienal, and (E,Z)-2,6-nonadienal were used to reveal the effect of the number and position of unsaturated bond in aliphatic aldehydes on Maillard reaction for the generation of 88 stewed meat-like volatile compounds. The results showed that (E,E)-2,4-nonadienal and (E,Z)-2,6-nonadienal exhibited greater inhibition of the cysteine reaction with glucose than nonanal and (E)-2-nonenal. However, the positions of the unsaturated bonds in aliphatic aldehydes in the Maillard reaction stage were similar. A carbohydrate module labeling approach was used to present the formation pathways of 34 volatile compounds derived from the Maillard reaction with aliphatic aldehyde systems. The number and position of unsaturated bonds in aliphatic aldehydes generate multiple pathways of flavor compound formation. 2-Propylfuran and (E)-2-(2-pentenyl)furan resulted from aliphatic aldehydes. 5-Butyldihydro-2(3H)-furanone and 2-methylthiophene were produced from the Maillard reaction. 2-Furanmethanol, 2-thiophenecarboxaldehyde, and 5-methyl-2-thiophenecarboxaldehyde were derived from the interaction of aliphatic aldehydes and the Maillard reaction. In Particular, the addition of aliphatic aldehydes changed the formation pathway of 2-propylthiophene, thieno[3,2-b]thiophene, and 2,5-thiophenedicarboxaldehyde. Heatmap and PLS-DA analysis could discriminate volatile compound compositions of the five systems and screen the marker compounds differentiating volatile compounds.

Topics: Aldehydes; Cysteine; Glucose

The interactions of soy protein isolate (SPI) and flavor compounds (hexanal, trans-2-hexenal, 1-octen-3-ol, trans-2-octenal, nonanal, and trans-2-nonenal) were investigated. The influence of SPI structure modified by malondialdehyde (MDA) and flavor compound structure on the interactions were determined by using headspace solid-phase microextraction (SPME) and gas chromatography (GC) combined with mass spectrometry (MS). The binding of native SPI to the flavor compounds decreased in the order trans-2-nonenal>nonanal>trans-2-octenal>trans-2-hexenal>hexanal>1-octen-3-ol. It might be attributed to that aldehydes are more hydrophobic than alcohols. The former is more conducive to hydrophobic binding with the SPI. Furthermore, the aldehydes, in particular trans-s-undecenal, could also react covalently. The effect of MDA modification on protein-flavor interactions depended on the structure of the flavor compound. Upon low concentration of MDA (≤1mM), the binding of all six flavors to SPI increased. However, a further increase in the extent of MDA (≥2.5mM), more soluble and even insoluble aggregates formed, which reduced the binding of hexanal and nonanal to SPI. The other four flavors with double bond revealed little changes in binding (trans-2-octenal, and trans-2-nonenal) or even an increase in binding (trans-2-hexenal, and 1-octen-3-ol). The results suggested that hydrophobic interactions were weakened upon high extent of oxidation, whereas covalent interactions were enhanced.

Topics: Alcohols; Aldehydes; Chromatography, Gas; Flavoring Agents; Hydrophobic and Hydrophilic Interactions; Malondialdehyde; Mass Spectrometry; Octanols; Odorants; Oxidation-Reduction; Particle Size; Solid Phase Microextraction; Soybean Proteins

The interactions of whey protein isolate (WPI) and flavor compounds (2-nonanone, 1-nonanal, and trans-2-nonenal) were investigated, and the influence of flavor compound structure and heat and high pressure denaturation on the interactions were determined by using headspace solid-phase microextraction (SPME) and gas chromatography (GC). The binding of WPI and the flavor compounds decreased in the order trans-2-nonenal > 1-nonanal > 2-nonanone. The differences in binding can be explained with hydrophobic interactions only in the case of 2-nonanone, whereas the aldehydes, in particular trans-2-nonenal, can also react covalently. Heat and high pressure treatment affected protein-flavor interactions depending on the structure of the flavor compound. Upon both heat and high pressure denaturation, the binding of 2-nonanone to WPI decreased, while the binding of 1-nonanal remained unchanged, and the affinity for trans-2-nonenal increased rapidly. The results suggest that hydrophobic interactions are weakened upon heat or high pressure denaturation, whereas covalent interactions are enhanced.

Topics: Aldehydes; Animals; Cattle; Flavoring Agents; Hot Temperature; Ketones; Milk Proteins; Pressure; Protein Binding; Solid Phase Microextraction; Whey Proteins

Transient activation of fibroblasts or fibroblast-like cells to proliferate and to produce elevated quantities of extracellular matrix is essential to fibrosis. This activation is regulated by several cytokines produced by various inflammation-associated cells. Among these, transforming growth factor beta1 (TGFbeta1) is considered of major importance. Many studies have shown that lipid peroxidation play a key role in the initiation and progression of fibrosis in different organs. In fact, 4-hydroxy-2,3-nonenal (HNE), the major aldehydic product of lipid peroxidation, is able to induce TGFbeta1 expression and synthesis, and activation of activator protein-1 (AP-1) transcription factor. In this study, using the murine macrophage line J774-A1, we show that these effects are strictly related to the chemical structure of HNE, since neither 2-nonenal nor nonanal are biologically active to the same extent. Moreover, we demonstrate that HNE can indeed contribute to the onset of fibrosis by stimulating AP-1 binding to DNA and consequently inducing TGFbeta1 expression, since thiol-group reagents, such as N-ethylmaleimide and 4-(chloro-mercuri)-benzenesulfonic acid, that down-modulate HNE entrance and localisation inside the cell, prevent both phenomena. The possibility to control fibrogenic cytokine levels by means of antioxidant or dietetic treatments opens new potential pharmacological and nutritional horizons in the treatment of many chronic diseases characterised by excessive fibrosis.

Topics: Aldehydes; Animals; Cell Line; DNA; Electrophoretic Mobility Shift Assay; Fibrosis; Gene Expression; Lipid Peroxidation; Macrophages; Mice; Proteins; Structure-Activity Relationship; Transcription Factor AP-1

The effects of three lipid peroxidation end-products, 4-hydroxynonenal (HNE), 2-nonenal (NE) and nonanal, on phosphoinositide-specific phospholipase C (PL-C) activity were studied in HL-60 cells. Enzymatic activity was determined by measuring the amounts of inositol-P3 (Ins-P3) produced by the cells incubated at 37 degrees C in the presence of the various compounds. HNE was shown to activate PL-C at concentrations of between 10(-8) and 10(-6) M; 10(-9) and 10(-8) M of NE also strongly stimulated PL-C. In contrast, nonanal failed to modify enzymatic activity. The concentrations of HNE and NE active on PL-C showed good correspondence with those that have been reported to be chemotactic towards rat neutrophils. The pretreatment of cells with 1 microM pertussis toxin completely prevented the increase of Ins-P3 production induced by HNE and NE. Maximal PL-C stimulation was produced by 10 nM NE; the degree of inositol-P3 production induced by the simultaneous addition of an equimolar dose of HNE was not significantly different from the activity value induced by NE alone, suggesting a possible competition between the two compounds. The data indicate that both HNE and NE share a common mechanism of action which, as with other better-known chemoattractants, involves PL-C activation through a G regulatory protein.

Topics: Aldehydes; Cysteine Proteinase Inhibitors; Dose-Response Relationship, Drug; Enzyme Activation; HL-60 Cells; Humans; Inositol 1,4,5-Trisphosphate; Kinetics; Lipid Peroxidation; Pertussis Toxin; Tumor Cells, Cultured; Type C Phospholipases; Virulence Factors, Bordetella

Aldehydes are known to inactivate cytochrome P450 in the reconstituted enzyme system containing NADPH and NADPH-cytochrome P450 reductase under aerobic conditions in a mechanism-based reaction involving heme adduct formation [Raner, G. M., Chiang, E. W. , Vaz, A. D. N., and Coon, M. J. (1997) Biochemistry 36, 4895-4902]. In the study presented here, artificial oxidants were used to examine the mechanism of aldehyde activation by purified P450 2B4 in the absence of the usual O(2)-reducing system, and the adducts that were formed were isolated and characterized. With hydrogen peroxide as the oxidant, 3-phenylpropionaldehyde gives an adduct with a mass corresponding to that of native heme modified by a phenylethyl group, presumably arising from the reaction of a peroxy-iron species with the aldehyde to give a peroxyhemiacetal, which upon deformylation yields the alkyl radical. NMR analysis indicated that the substitution is specifically at the gamma-meso position. In contrast, with m-chloroperbenzoic acid as the oxidant, an adduct is formed from 3-phenylpropionaldehyde with a mass that is consistent with the addition of a phenylpropionyl group, apparently arising by hydrogen abstraction from the aldehyde to give the carbonyl carbon radical. m-Chloroperbenzoic acid by itself forms a heme adduct with a mass corresponding to the addition of a chlorobenzoyloxy group apparently derived from homolytic oxygen-oxygen bond cleavage. These and other results with nonanal and 2-trans-nonenal support the concept that this versatile enzyme utilizes discrete oxidizing species in heme adduct formation from aldehydes.

Topics: Aldehydes; Animals; Cytochrome P-450 Enzyme System; Heme; Hydrogen Peroxide; Microsomes, Liver; Nuclear Magnetic Resonance, Biomolecular; Oxidants; Rabbits; Reactive Oxygen Species; Spectrophotometry, Ultraviolet

The effects of nonanal, trans-2-nonenal and 4-hydroxy-2,3-trans-nonenal on the formation of thromboxane B2 (TXB2), 12-hydroxy-5,8,10-heptadecatrienoic acid (HHT) and 12-hydroxy-5,8,10,14-eicosatetraenoic acid (12-HETE) from exogenous arachidonic acid in washed rabbit platelets were examined. Nonanal and trans-2-nonenal at concentrations ranging from 0.25 to 2 microM inhibited TXB2, HHT and 12-HETE formation, reducing the amounts of these three arachidonic acid metabolites by 50% at nonanal and trans-2-nonenal concentrations of approximately 0.25 microM. The inhibition of TXB2, HHT and 12-HETE formation induced by 4-hydroxy-2,3-trans-nonenal (50% inhibition by 4-hydroxy-2,3-trans-nonenal at a concentration of approximately 100 microM) was 400 times weaker than that induced by nonanal and trans-2-nonenal. These results suggest that nonanal and trans-2-nonenal can be modulators of platelet arachidonic acid metabolism by affecting the activity of cyclooxygenase and 12-lipoxygenase.

Topics: Aldehydes; Animals; Arachidonic Acid; Blood Platelets; Cyclooxygenase Inhibitors; Lipoxygenase Inhibitors; Male; Rabbits