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PubMed1996

Inactivation of glutathione peroxidase by benzaldehyde.

Chronic benzaldehyde exposure is known to cause central nervous system (CNS) disturbances. Previous studies have shown that benzaldehyde causes the formation of reactive oxygen species (ROS) in rat synaptosomal fractions. Benzaldehyde has also been implicated in ROS formation in the CNS of rats treated with toluene. We have found that benzaldehyde effectively inactivates the antioxidant enzyme glutathione peroxidase (Ki approximately 15 microM), but has no effect on the other antioxidant enzymes tested: catalase, superoxide dismutase, and glutathione reductase. This effect has been found to be specific to benzaldehyde since other structurally related and unrelated aldehydes tested were found to be devoid of inactivating capacity toward glutathione peroxidase. Since glutathione peroxidase is the main enzyme responsible for removal of hydrogen peroxide and organic hydroperoxides in brain, its inactivation by benzaldehyde may be a main contributor to the observed ROS formation and the observed neurotoxicity caused by either benzaldehyde or toluene exposure.

Animals↗
PubMed1984

Reduction of cis-dichlorodiammineplatinum-induced cell inactivation by benzaldehyde.

The inactivating effect of a combined treatment of human cells (NHIK 3025) in culture with cis-dichlorodiammineplatinum(II) (cis-DDP) and the protein synthesis inhibitor benzaldehyde was tested. Cell inactivation was measured as loss of colony-forming ability following drug treatment. While 3.2 mM benzaldehyde had no effect on the cell survival when given alone, it reduced the effect of 10 microM cis-DDP significantly when the two drugs were added simultaneously. Scheduling experiments indicate that benzaldehyde must be present immediately before addition of, or simultaneously with, cis-DDP for optimal reduction of cell inactivation. Benzoic acid, benzyl alcohol or the protein synthesis inhibitor cycloheximide did not reduce the inactivating effect of cis-DDP. Cells synchronized by mitotic selection were used to determine the variation in the responses throughout the cell cycle. It was found that concomitant 2-hr treatment of synchronized cells with 3.2 mM benzaldehyde and 10 microM cis-DDP at various times during the cell cycle resulted in a consistently greater surviving fraction of cells than 10 microM cis-DDP alone. Benzaldehyde thus reduced the inactivating effect of cis-DDP in all phases of the cell cycle. The effect of benzaldehyde in combination with two alkylating agents, 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU) and nitrogen mustard (HN2), was also studied. Benzaldehyde was not found to influence the effects on cell survival induced by these drugs.

Benzaldehydes↗
PubMed2006

Enhanced benzaldehyde tolerance in Zymomonas mobilis biofilms and the potential of biofilm applications in fine-chemical production.

Biotransformation plays an increasingly important role in the industrial production of fine chemicals due to its high product specificity and low energy requirement. One challenge in biotransformation is the toxicity of substrates and/or products to biocatalytic microorganisms and enzymes. Biofilms are known for their enhanced tolerance of hostile environments compared to planktonic free-living cells. Zymomonas mobilis was used in this study as a model organism to examine the potential of surface-associated biofilms for biotransformation of chemicals into value-added products. Z. mobilis formed a biofilm with a complex three-dimensional architecture comprised of microcolonies with an average thickness of 20 microm, interspersed with water channels. Microscopic analysis and metabolic activity studies revealed that Z. mobilis biofilm cells were more tolerant to the toxic substrate benzaldehyde than planktonic cells were. When exposed to 50 mM benzaldehyde for 1 h, biofilm cells exhibited an average of 45% residual metabolic activity, while planktonic cells were completely inactivated. Three hours of exposure to 30 mM benzaldehyde resulted in sixfold-higher residual metabolic activity in biofilm cells than in planktonic cells. Cells inactivated by benzaldehyde were evenly distributed throughout the biofilm, indicating that the resistance mechanism was different from mass transfer limitation. We also found that enhanced tolerance to benzaldehyde was not due to the conversion of benzaldehyde into less toxic compounds. In the presence of glucose, Z. mobilis biofilms in continuous cultures transformed 10 mM benzaldehyde into benzyl alcohol at a steady rate of 8.11 g (g dry weight)(-1) day(-1) with a 90% molar yield over a 45-h production period.

Benzaldehydes↗
PubMed2005

Influence of thermal processing conditions on flavor stability in fluid milk: benzaldehyde.

Flavor loss in dairy products has been associated with enzymatic degradation by xanthine oxidase. This study was conducted to investigate the influence of milk thermal processing conditions (or xanthine oxidase inactivation) on benzaldehyde stability. Benzaldehyde was added to whole milk which had been thermally processed at 4 levels: (1) none or raw, (2) high temperature, short time (HTST) pasteurization, (3) HTST pasteurization, additionally heated to 100 degrees C (PAH), and (4) UHT sterilized. Additionally, PAH and UHT milk samples containing benzaldehyde (with and without ferrous sulfate) were spiked with xanthine oxidase. Azide was added as an antimicrobial agent (one additional pasteurized sample without) and the microbial load (total plate count) was determined on d 0, 2, and 6. The concentration of benzaldehyde and benzoic acid in all milk samples were determined at d 0, 1, 2, 4, and 6 (stored at 5 degrees C) by gas chromatography/mass spectrometry in selective ion monitory mode. Over the 6-d storage period, more than 80% of the benzaldehyde content was converted (oxidized) to benzoic acid in raw and pasteurized milk, whereas no change in the benzaldehyde concentration was found in PAH or UHT milk samples. Furthermore, the addition of xanthine oxidase or xanthine oxidase plus ferrous sulfate to PAH or UHT milk samples did not result in benzaldehyde degradation over the storage period.

Animals↗
PubMedDate not supplied

Reduced cellular uptake of cis-dichlorodiammine-platinum by benzaldehyde.

Synchronized human NHIK 3025 cells were treated with cis-dichlorodiammineplatinum (cis-DDP) either alone or in combination with benzaldehyde as a 2 h pulse in G1-phase. After this pulse, the cells entered S-phase and the rate of DNA synthesis was measured by DNA-flow cytometric recordings of serial samples. After treatment with 10 microM cis-DDP alone, the rate of DNA synthesis was 38% of the control rate. If 3.2 mM benzaldehyde was present together with 10 microM cis-DDP, the rate of DNA synthesis was 56% of the control rate, this being similar to the rate measured following treatment of cells with 5 microM cis-DDP alone. Thus, the simultaneous presence of benzaldehyde with cis-DDP mitigates the inhibition of DNA synthesis induced by cis-DDP. However, when cells were electropermeabilized during the treatment pulse, benzaldehyde did not protect the cells from cis-DDP-induced cell inactivation. The protective effect of benzaldehyde thus seems to reside with the cell membrane and it seems that benzaldehyde, when present together with cis-DDP, partially inhibits the uptake of cis-DDP into cells. Atomic absorption spectroscopy confirmed that the simultaneous presence of 5 mM benzaldehyde halved the amount of cell-bound platinum from that measured following treatment with cis-DDP alone.

Benzaldehydes↗
PubMed1983

Effects of benzaldehyde on survival and cell-cycle kinetics of human cells cultivated in vitro.

Synchronized cells of the human line NHIK 3025 were used to study inactivating and cell-cycle inhibitory effects induced by benzaldehyde. Inactivation was measured as loss of colony-forming ability after treatment of exponentially growing or synchronized cells. Cell-cycle inhibition was measured by flow cytometric recordings of DNA-histograms and microscopic recordings of cell division in synchronized cells. Treatment with benzaldehyde for 4 or 24 hr showed that a marked decrease in survival took place for concentrations above 6.4 mM. Cell-cycle inhibition was observed at concentrations as low as 0.8 mM. Synchronized cells were treated with 3.2 and 6.4 mM benzaldehyde for 8 hr starting at various stages of the cell-cycle. Both the colony-forming ability and the rate of cell-cycle traverse was measured. No difference in sensitivity was found whether the treatment was given in G1, S or in G2. Thus the results show that there is no specific part of interphase where the cells are particularly sensitive with respect to either the inactivating or the cell-cycle inhibitory effects of benzaldehyde in concentrations up to 6.4 mM. When benzaldehyde was present during mitosis both the inactivating and the cell-cycle inhibitory effects were markedly enhanced as compared to the corresponding effects during interphase. It is concluded that benzaldehyde must affect some process within the cell which represents a general requirement for cell-cycle progression. In addition, there are effects on processes that take place only during the last few minutes before and/or during mitosis.

Benzaldehydes↗
PubMed2005

Role of pyruvate in enhancing pyruvate decarboxylase stability towards benzaldehyde.

Biotransformation of benzaldehyde and pyruvate into (R)-phenylacetylcarbinol (PAC) catalysed by Candida utilis pyruvate decarboxylase (PDC) at low buffer concentration (20 mM MOPS) was enhanced by maintenance of neutral pH through acetic acid addition. PDC was very stable in this buffer (half-life 138 h at 6 degrees C), however a benzaldehyde emulsion (400 mM) caused rapid deactivation. The inclusion of 2M glycerol did not protect PDC from inactivation by benzaldehyde but initial rates were increased by 50% and the final PAC level was enhanced from 40 to 51 g l(-1). Low levels of by-products acetaldehyde (0.1-0.15 g l(-1)) and acetoin (1.1-1.3 g l(-1)) were formed in both the presence and absence of 2 M glycerol. Interestingly PDC was more stable towards benzaldehyde when pyruvate was present: no activity was lost during the first hour of biotransformation (2 M glycerol, benzaldehyde concentration decreased from 400 to 345 mM, pyruvate from 480 to 420 mM) but PDC was completely inactivated in less than 30 min when exposed to the same concentrations of benzaldehyde in the absence of pyruvate. Thus the enzyme in catalytic action was more stable than the resting enzyme.

Acetone↗
PubMed1987

Labeling of bovine heart cytochrome c oxidase with analogues of phospholipids. Synthesis and reactivity of a new cardiolipin benzaldehyde probe.

The syntheses of two new radioactive probes derived from cardiolipin and phosphatidylcholine are reported. These probes are derivatives of natural lipids and contain an amine-specific benzaldehyde in the head-group region. This functional group allows a choice of timing of the reaction (e.g., after equilibration and detergent removal) because an irreversible covalent bond is formed only upon the addition of reducing agent. These probes, as well as a benzaldehyde analogue of phosphatidic acid, and a water-soluble benzaldehyde reagent were covalently attached to bovine heart cytochrome c oxidase. After reconstitution into vesicles, the lipid-benzaldehyde probes selectively incorporated into the smaller polypeptides of the enzyme, while the remaining subunits (I-IV) exhibited little incorporation of label. The accessibility of amine groups labeled under the conditions used here was independent of the structural and charge differences between the benzaldehyde probes. This suggests that all three lipid probes react with polypeptides of the cytochrome c oxidase complex at general contact sites for membrane phospholipids. A water-soluble benzaldehyde reagent predominantly labeled subunits IV, Va, and Vb and polypeptides of VII-VIII. A comparison of these results facilitates a more refined view of the disposition of polypeptides of cytochrome c oxidase in respect to the lipid and aqueous phases.

Animals↗
PubMed1992

Benzaldehyde, citral, and d-limonene flavor perception in the presence of casein and whey proteins.

The effect of sodium caseinate and whey protein concentrate on benzaldehyde, d-limonene, and citral flavor intensity was determined by quantitative descriptive analysis deviation from reference using a 12-member trained panel. The concentrations for the benzaldehyde, d-limonene, and citral flavor intensity references were 17.8, 53.0, and 19.8 ppm, respectively. The concentration for both protein references was .25%. Flavored protein solutions were held for 17 h at 6 degrees C and contained benzaldehyde (17.8 ppm), d-limonene (53 ppm), or citral (19.8 ppm) and 2.5% sucrose with 0, .125, .25, or .5% protein. Benzaldehyde flavor intensity declined as the whey protein concentrate concentration increased from 0 to .5%. There was no significant difference in benzaldehyde flavor intensity with casein compared with the reference. The d-limonene flavor intensity declined as the protein concentration increased. Panelists found no significant drop in citral flavor intensity with casein or whey protein. Decreased benzaldehyde and d-limonene flavor intensity in the presence of whey protein concentrate or casein may be due to nonpolar interactions (casein), interaction with nonpolar binding sites, cysteine-aldehyde condensation, or Schiff base formation (whey protein concentrate).

Acyclic Monoterpenes↗
PubMedDate not supplied

Effect on protein synthesis and cell survival of the benzaldehyde derivatives sodium benzylidene ascorbate (SBA) and the deuterated compound zilascorb(2H).

Three different benzaldehyde derivatives (viz. beta-cyclodextrin benzaldehyde inclusion compound (CDBA), 4, 6-O-benzylidene-D-glucose (BG) and sodium benzylidene-ascorbate (SBA) have been shown to exert anticancer effects in patients without causing side effects. The anticancer effects are, however, variable and in many cases weak. In a previous study we showed that benzaldehyde with a deuterated formyl group gave rise to a greater protein synthesis inhibition than nondeuterated benzaldehyde. Based on this deuterated benzaldehyde we have synthesized an ascorbic acid acetal; 5,6-benzylidene-d1-L-ascorbic acid (zilascorb(2H). In the present paper we compare the effect of this drug with respect to cell inactivation and inhibition of protein synthesis in human cells cultured in vitro with that of benzaldehyde, BG and SBA. It is shown that zilascorb (2H) is clearly the most effective of these drugs. The effect of zilascrob(2H) is reversible in the sense that protein synthesis regains its normal level shortly (i.e. within 1h) after removal of the drug. Even after protracted treatment inducing a cell kill of more than 99%, the few survivors appear to be without damage after removal of the drug.

Antineoplastic Agents↗
PubMed1996

Detection and Reaction of Oxaphosphetanes Derived from Benzaldehyde and 1-Adamantylmethylidene Ylide.

The Wittig reaction of (1-adamantylmethylidene)triphenylphosphorane (Ph(3)P=CH(1-Ad)) with benzaldehyde was investigated, and the results were compared with those of other ylides. The substituent effect in the reaction of the ylide with benzaldehydes was determined by competition experiments, which gave a Hammett rho value of 3.2. The rho value is much larger than those reported for analogous reactions of Ph(3)P=CH(CH(2))(2)CH(3) (rho = 0.20) and Ph(3)P=CH(CH(3))(2) (rho = 0.59), indicating that the reaction mechanism differs for Ph(3)P=CH(1-Ad) and the other ylides. The cis/trans ratio of the product alkene is 74/26 for the reaction with the parent benzaldehyde and highly depends on the position of the substituent; ortho substituted benzaldehydes gave the trans alkenes up to 90%. Monitoring the reaction by means of (31)P NMR revealed that both cis and trans oxaphosphetane intermediates were formed and that the formation and decomposition of the cis oxaphosphetane are 7-12 times faster than those of the trans oxaphosphetane. From the comparison of the reaction of Ph(3)P=CH(1-Ad) + benzaldehyde with those of Ph(3)P=CH(CH(2))(2)CH(3) + benzaldehyde and benzophenone, and Ph(3)P=CH(CH(3))(2) + benzophenone, it was concluded that all the reactions with these nonstabilized ylides proceed via an electron-transfer mechanism and that the rate-determining step changes from the electron transfer step to that of radical combination when the substrate or ylide becomes more sterically demanding.

Journal Article↗
PubMed2000

Kinetics and mechanism of the oxidation of substituted benzaldehydes by benzyltrimethylammonium chlorobromate

The oxidation of 35 monosubstituted benzaldehydes by benzyltrimethylammonium chlorobromate (BTMACB) in aqueous acetic acid leads to the formation of the corresponding benzoic acids. The reaction is first order with respect to both benzaldehyde and BTMACB. The reaction failed to induce the polymerization of acrylonitrile. There is no effect of benzyltrimethylammonium chloride or potassium bromide on the reaction rate. The oxidation of [(2)H]benzaldehyde (PhCDO) indicated the presence of a substantial kinetic isotope effect. The effect of solvent composition indicated that the reaction rate increases with an increase in the polarity of the solvent. The rates of oxidation of meta- and para-substituted benzaldehydes were correlated in terms of Charton's triparametric LDR equation, whereas the oxidation of ortho-substituted benzaldehydes was correlated with the tetraparametric LDRS equation. The oxidation of para-substituted benzaldehydes is more susceptible to the delocalization effect, whereas the oxidation of ortho-and meta-substituted compounds displayed a greater dependence on the field effect. The positive value of eta suggests the presence of an electron-deficient reaction center in the rate-determining step. The reaction is subjected to steric hindrance by the ortho substituents.

Journal Article↗
PubMed1995

Identification of 4-(N,N-dipropylamino)benzaldehyde as a potent, reversible inhibitor of mouse and human class I aldehyde dehydrogenase.

As the physiologic roles for the different classes of aldehyde dehydrogenase (ALDH) enzymes are elucidated, the identification of specific, reversible inhibitors becomes of great pharmacologic interest. Previous structure-function studies identified dialkylamino substituted benzaldehyde compounds as a novel class of reversible inhibitors of class I ALDH. To examine further structural requirements for inhibition, we tested a series of 4-(N,N-dialkylamino)benzaldehyde analogs as inhibitors of propanal oxidation by mouse liver and human erythrocyte class I ALDH. 4-(N,N-dipropylamino)benzaldehyde (DPAB) was identified as the most potent, reversible inhibitor of propanal oxidation by class I ALDH in spectrophotometric enzyme assays. In kinetic studies, DPAB showed mixed-type inhibition with respect to the aldehyde substrates propanal, phenylacetaldehyde, benzaldehyde, and aldophosphamide. DPAB exhibited uncompetitive inhibition with respect to the cofactor NAD. Inhibition constants (Ki) for DPAB, estimated from Dixon plots, were 10 nM (propanal) and 77 nM (phenylacetaldehyde) for mouse ALDH and 3 nM (propanal) and 70 nM (phenylacetaldehyde) for human ALDH. These Ki values are 100-fold lower than those reported for class I specific inhibitors. At low (< 1 microM) DPAB concentrations, inhibition of propanal and aldophosphamide oxidation was > 75%, whereas inhibition of benzaldehyde (32%) and phenylacetaldehyde (19%) oxidation was reduced markedly. These results indicate that DPAB exhibits potent, reversible inhibition of mouse and human class I ALDH. The degree of inhibition was highly dependent on the structure of the aldehyde substrate.

Acetaldehyde↗
PubMed1994

Gas-liquid chromatographic and difference spectrophotometric techniques for the determination of benzaldehyde in benzyl alcohol.

Simple, sensitive, rapid and selective gas-liquid chromatographic and difference spectrophotometric methods have been described for the determination of benzaldehyde, an oxidation product of benzyl alcohol, in benzyl alcohol intended for use in the manufacture of parenteral dosage forms. The GLC method comprises chromatography of a mixture of benzaldehyde and benzyl alcohol on a CP-Sil5 WSCOT capillary column after dilution with chloroform and addition of 4-chlorocresol as the internal standard, using nitrogen as the mobile phase and a flame ionization detector. The difference spectrophotometric method involves the measurement of the absorbance of benzaldehyde relative to an equimolar solution in which benzaldehyde has been reduced by sodium borohydride. Both methods are accurate, precise and selective for the determination of benzaldehyde in benzyl alcohol in the presence of benzoic acid, a second oxidation product of benzyl alcohol.

Anti-Infective Agents, Local↗
PubMed2004

O-Methylation of benzaldehyde derivatives by "lignin specific" caffeic acid 3-O-methyltransferase.

Although S-adenosyl-l-methionine (SAM) dependent caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase (COMT) is one of the key enzymes in lignin biosynthesis, the present work demonstrates that alfalfa COMT methylates benzaldehyde derivatives more efficiently than lignin pathway intermediates. 3,4-Dihydroxy, 5-methoxybenzaldehyde and protocatechuic aldehyde were the best in vitro substrates for OMT activity in extracts from developing alfalfa stems, and these compounds were preferred over lignin pathway intermediates for 3-O-methylation by recombinant alfalfa COMT expressed in Escherichia coli. OMT activity with benzaldehydes was strongly reduced in extracts from stems of transgenic alfalfa down-regulated in COMT. However, although COMT down-regulation drastically affects lignin composition, it does not appear to significantly impact metabolism of benzaldehyde derivatives in alfalfa. Structurally designed site-directed mutants of COMT showed altered relative substrate preferences for lignin precursors and benzaldehyde derivatives. Taken together, these results indicate that COMT may have more than one role in phenylpropanoid metabolism (but probably not in alfalfa), and that engineered COMT enzymes could be useful for metabolic engineering of both lignin and benzaldehyde-derived flavors and fragrances.

Amino Acid Substitution↗
PubMed2003

Capillary gas chromatography determination of benzaldehyde arising from benzyl alcohol used as preservative in injectable formulations.

A simple, precise and accurate capillary gas-liquid chromatographic procedure has been developed to determine benzaldehyde, the toxic oxidation product of the widely used preservative and co-solvent benzyl alcohol, in injectable formulations of the non-steroidal anti-inflammatory drugs, diclofenac and piroxicam, as well as in Vitamin B-complex injection solutions. Following liquid-liquid extraction with chloroform, separation and quantification are achieved on a fused silica capillary column (25 m x 0.53 mm i.d.) coated with 0.5 microm film of OV-101. 3-Chlorobenzaldehyde was used as internal standard with flame-ionization as the detection mode. The ability of the system to resolve benzaldehyde peak from interfering components is good. The method displays excellent linearity over the concentration range 0.5-100 microg/ml of benzaldehyde and a precision of better than 2.5% from intra- and inter-day analyses. The quantification limit for benzaldehyde is 0.4 microg/ml. Levels of benzaldehyde in generic diclofenac and piroxicam injection formulations were found to be seven to 15 times higher than in reference formulations, and double in generic Vitamin B-complex injection formulations.

Benzaldehydes↗
PubMed1998

QSARs for the effect of benzaldehydes on foodborne bacteria and the role of sulfhydryl groups as targets of their antibacterial activity.

Quantitative structure activity relationships (QSARs) were obtained describing the activity of a series of benzaldehydes against three different foodborne bacteria, Listeria monocytogenes F6861, serotype 4b, Salmonella enteritidis, Phage type 4, P167807 and Lactobacillus plantarum INT.L11. MIC values at pH 6.2 and 35 degrees C were obtained for 11 phenolic benzaldehydes to produce multiple linear regression and artificial neural network models. For each organism, the models contained a steric parameter Vw and an electronic-steric parameter for ortho substituents Es degree. The benzaldehydes did not require to partition to produce their effect, shown by the lack of a lipophilic parameter in the models. This strongly suggests that they act on the outside of the cells. Substitution ortho to the carbonyl group increased their antibacterial action. Cells were treated with 2,3-dihydroxy benzaldehyde and examined for their ability to bind radiolabelled iodoacetate to envelope sulfhydryl groups that remained available. It was shown that the accumulation of radiolabelled iodoacetate was lower after treatment, indicating possible competition between these two compounds for the same target. The order of the sensitivity to benzaldehydes (Salmonella > Listeria > Lactobacillus) correlated with the number of surface sulfhydryl groups available, being highest for Salmonella.

Anti-Bacterial Agents↗
PubMed2001

Shifting the biotransformation pathways of L-phenylalanine into benzaldehyde by Trametes suaveolens CBS 334.85 using HP20 resin.

AIMS: The biotransformation of L-phenylalanine into benzaldehyde (bitter almond aroma) was studied in the strain Trametes suaveolens CBS 334.85. METHODS AND RESULTS: Cultures of this fungus were carried out in the absence or in the presence of HP20 resin, a highly selective adsorbent for aromatic compounds. For the identification of the main catabolic pathways of L-phenylalanine, a control medium (without L-phenylalanine) was supplemented with each of the aromatic compounds, previously detected in the culture broth, as precursors. Trametes suaveolens CBS 334.85 was shown to biosynthesize benzyl and p-hydroxybenzyl derivatives, particularly benzaldehyde, and large amounts of 3-phenyl-1-propanol, benzyl and p-hydroxybenzyl alcohols as the products of both cinnamate and phenylpyruvate pathways. CONCLUSION: The addition of HP20 resin, made it possible to direct the catabolism of L- phenylalanine to benzaldehyde, the desired target compound, and to trap it before its transformation into benzyl alcohol. In these conditions, benzaldehyde production was increased 21-fold, from 33 to 710 mg l-1 corresponding to a molar yield of 31%. SIGNIFICANCE AND IMPACT OF THE STUDY: These results showed the good potential of Trametes suaveolens as a biotechnological agent to synthesize natural benzaldehyde which is one of the most important aromatic aldehydes used in the flavour industry.

Benzaldehydes↗