Alcohol Aldehyde Research Articles

Recent Advances in Research into Jasmonate Biosynthesis and Signaling Pathways in Agricultural Crops and Products

Jasmonates (JAs) are phospholipid-derived hormones that regulate plant development and responses to environmental stress. The synthesis of JAs and the transduction of their signaling pathways are precisely regulated at multiple levels within and outside the nucleus as a result of a combination of genetic and epigenetic regulation. In this review, we focus on recent advances in the regulation of JA biosynthesis and their signaling pathways. The biosynthesis of JAs was found to be regulated with an autocatalytic amplification mechanism via the MYC2 regulation pathway and inhibited by an autonomous braking mechanism via the MYC2-targeting bHLH1 protein to terminate JA signals in a highly ordered manner. The biological functions of JAs mainly include the promotion of fruit ripening at the initial stage via ethylene-dependent and independent ways, the regulation of mature coloring via regulating the degradation of chlorophyll and the metabolism of anthocyanin, and the improvement of aroma components via the regulation of fatty acid and aldehyde alcohol metabolism in agricultural crops. JA signaling pathways also function in the enhancement of biotic and abiotic stress resistance via the regulation of secondary metabolism and the redox system, and they relieve cold damage to crops through improving the stability of the cell membrane. These recently published findings indicate that JAs are an important class of plant hormones necessary for regulating plant growth and development, ripening, and the resistance to stress in agricultural crops and products.

Portable SERS sensing of volatile aldehydes in alcohols by aldol condensation reaction on liquid interfacial plasmonic arrays.

An aldol condensation reaction on oil-in-water (O/W) liquid interfacial plasmonic arrays was developed for sensing volatile aldehydes in alcohols by using an aromatic aldehyde as the probe for portable SERS assays. The detection limit was 10-8 M. The substrate exhibited an RSD value of 6.9%, and the probe showed good selectivity to four common interferences.

Densities and Viscosities for Binary Liquid Mixtures of n-Aldehydes + Ethanol from 283.15 to 343.15 K at 0.1 MPa

This work reports densities and viscosities of four binary mixtures of aldehydes (C7–C10) + ethanol from 283.15 to 343.15 K at 0.1 MPa. A vibrating tube densimeter is used to measure the experimental densities, while a rolling ball microviscometer measures the dynamic viscosity. Excess molar volumes and viscosity deviations are calculated from the experimental densities and viscosities, respectively. Excess molar volumes show negative deviations, while viscosity deviations are positive. The behavior of these derived properties reflects the formation of hemiacetals by the interaction of the carbonyl and the hydroxyl group as reported in the literature. The aldehyde–alcohol interaction becomes weaker as the temperature rises, reflected in the data behavior. A Redlich–Kister equation is used to correlate both the excess molar volume and the viscosity deviation, within average absolute percentage deviations of 2.738 and 5.928%, respectively. Kinematic viscosities are correlated using the three-body and four-body McAllister equations and the Nava-Ríos equation. The average absolute percentage deviations from the experimental measurements are 2.07, 0.99, and 1.22%, respectively.

Is There Any Linkage between Interstellar Aldehyde and Alcohol?

Abstract It is speculated that there might be some linkage between interstellar aldehydes and their corresponding alcohols. Here an observational study and astrochemical modeling are coupled together to illustrate the connection between them. The ALMA cycle 4 data of a hot molecular core, G10.47+0.03, are utilized for this study. Various aldehydes (acetaldehyde, propanal, and glycolaldehyde), alcohols (methanol and ethylene glycol), and a ketone (acetone) are identified in this source. The excitation temperatures and column densities of these species were derived via the rotation diagram method assuming local thermodynamic equilibrium conditions. An extensive investigation is carried out to understand the formation of these species. Six pairs of aldehyde–alcohol are considered for this study: (i) methanal and methanol, (ii) ethanal and ethanol, (iii) propanal and 1-propanol, (iv) propenal and allyl alcohol, (v) propynal and propargyl alcohol, and (vi) glycolaldehyde and ethylene glycol. One pair of ketone–alcohol (acetone and isopropanol) and ketene–alcohol (ethenone and vinyl alcohol) are also considered. Two successive hydrogenation reactions in the ice phase are examined to form these alcohols from aldehydes, ketone, and ketene, respectively. Quantum chemical methods are extensively executed to review the ice-phase formation route and the kinetics of these species. Based on the obtained kinetic data, astrochemical modeling is employed to derive the abundances of these aldehydes, alcohols, ketone, and ketene in this source. It is seen that our model could successfully explain the observed abundances of various species in this hot molecular core.

In vitro metabolism of HMTD and blood stability and toxicity of peroxide explosives (TATP and HMTD) in canines and humans

Triacetone triperoxide (TATP) and hexamethylene triperoxide diamine (HMTD) are prominent explosive threats. Mitigation of peroxide explosives is a priority among the law enforcement community, with canine (K9) units being trained to recognise the scent of peroxide explosives. Herein, the metabolism, blood distribution, and toxicity of peroxide explosives are investigated. HMTD metabolism studies in liver microsomes identified two potential metabolites, tetramethylene diperoxide diamine alcohol aldehyde (TMDDAA) and tetramethylene peroxide diamine dialcohol dialdehyde (TMPDDD). Blood stability studies in dogs and humans showed that HMTD was rapidly degraded, whereas TATP remained for at least one week. Toxicity studies in dog and human hepatocytes indicated minimum cell death for both TATP and HMTD.

Combined evolutionary engineering and genetic manipulation improve low pH tolerance and butanol production in a synthetic microbial Clostridium community.

Synthetic microbial communities have become a focus of biotechnological research since they can overcome several of the limitations of single-specie cultures. A paradigmatic example is Clostridium cellulovorans DSM 743B, which can decompose lignocellulose but cannot produce butanol. Clostridium beijerinckii NCIMB 8052 however, is unable to use lignocellulose but can produce high amounts of butanol from simple sugars. In our previous studies, both organisms were cocultured to produce butanol by consolidated bioprocessing. However, such consolidated bioprocessing implementation strongly depends on pH regulation. Since low pH (pH 4.5-5.5) is required for butanol fermentation, C. cellulovorans cannot grow well and saccharify sufficient lignocellulose to feed both strains at a pH below 6.4. To overcome this bottleneck, this study engineered C. cellulovorans by adaptive laboratory evolution, inactivating cell wall lyases genes (Clocel_0798 and Clocel_2169), and overexpressing agmatine deiminase genes (augA, encoded by Cbei_1922) from C. beijerinckii NCIMB 8052. The generated strain WZQ36: 743B*6.0*3△lyt0798△lyt2169-(pXY1-Pthl -augA) can tolerate a pH of 5.5. Finally, the alcohol aldehyde dehydrogenase gene adhE1 from Clostridium acetobutylicum ATCC 824 was introduced into the strain to enable butanol production at low pH, in coordination with solvent fermentation of C. beijerinckii in consortium. The engineered consortium produced 3.94 g/L butanol without pH control within 83 hr, which is more than5-fold of the level achieved by wild consortia under the same conditions. This exploration represents a proof of concept on how to combine metabolic and evolutionary engineering to coordinate coculture of a synthetic microbial community.

Metabolic Engineering of Clostridium cellulovorans to Improve Butanol Production by Consolidated Bioprocessing.

Clostridium cellulovorans DSM 743B can produce butyrate when grown on lignocellulose, but it can hardly synthesize butanol. In a previous study, C. cellulovorans was successfully engineered to switch the metabolism from butyryl-CoA to butanol by overexpressing an alcohol aldehyde dehydrogenase gene adhE1 from Clostridium acetobutylicum ATCC 824; however, its full potential in butanol production is still unexplored. In the study, a metabolic engineering approach based on a push-pull strategy was developed to further enhance cellulosic butanol production. In order to accomplish this, the carbon flux from acetyl-CoA to butyryl-CoA was pulled by overexpressing a trans-enoyl-coenzyme A reductase gene (ter), which can irreversibly catalyze crotonyl-CoA to butyryl-CoA. Then an acid reassimilation pathway uncoupled with acetone production was introduced to redirect the carbon flow from butyrate and acetate toward butyryl-CoA. Finally, xylose metabolism engineering was implemented by inactivating xylR (Clocel_0594) and araR (Clocel_1253), as well as overexpressing xylT (CA_C1345), which is expected to supply additional carbon and reducing power for CoA and butanol synthesis pathways. The final engineered strain produced 4.96 g/L of n-butanol from alkali extracted corn cobs (AECC), increasing by 235-fold compared to that of the wild type. It serves as a promising butanol producer by consolidated bioprocessing.

Four interpenetrating hydrogen-bonded three-dimensional networks in divanillin

The crystal structure of divainillin (systematic name: 6,6'-dihydroxy-5,5'-dimethoxy-[1,1'-biphenyl]-3,3'-dicarbaldehyde), C16H14O6, was determined from laboratory powder X-ray diffraction data using the software EXPO2013 (direct methods) and WinPSSP (direct-space approach). Divanillin molecules crystallize in the orthorhombic space group Pba2 (No. 32), with two molecules per unit cell (Z' = 1/2). Each divanillin molecule, with twofold symmetry, is linked through strong alcohol-aldehyde hydrogen bonds to four equivalent molecules, defining a three-dimensional hydrogen-bonding network, with rings made up of six divanillin units (a diamond-like arrangement). Each molecule is also connected through π-π interactions to a translation-equivalent molecule along c. Four consecutive molecules stacked along [001] belong to four different three-dimensional hydrogen-bonding networks defining a quadruple array of interpenetrating networks. This complex hydrogen-bonding array is proposed as an explanation for the aging process experienced by divanillin powders.

Unexpected Composition Dependence of the First Sharp Diffraction Peak in an Alcohol–Aldehyde Liquid Mixture: n‐Pentanol and Pentanal

The total scattering structure factors of pure liquid n‐pentanol, pentanal, and five of their mixtures, as determined by high energy synchrotron X‐ray diffraction experiments, are presented. For the interpretation of measured data, molecular dynamics computer simulations are performed, utilizing “all‐atom” type force fields. The diffraction signals in general resemble each other over most of the monitored scattering variable, Q, range above 1 Å−1, but the absolute values of the intensities of the small‐angle scattering maximum (“pre‐peak,” “first sharp diffraction peak”), around 0.6 Å−1, change in an unexpected fashion, non‐linearly with the composition. Molecular dynamics simulations are not able to reproduce this low‐Q behavior; on the other hand, they do reproduce the experimental diffraction data above 1 Å−1 rather accurately. Partial radial distribution functions are calculated based on the atomic coordinates in the simulated configurations. Inspection of the various OO and OH partial radial distribution functions clearly shows that both the alcoholic and the aldehydic oxygens form hydrogen bonds with the hydrogen atoms of the alcoholic OH‐group.

The bifunctional aldehyde–alcohol dehydrogenase controls ethanol and acetate production in Entamoeba histolytica under aerobic conditions

By applying metabolic control analysis and inhibitor titration we determined the degree of control (flux control coefficient) of pyruvate:ferredoxin oxidoreductase (PFOR) and bifunctional aldehyde–alcohol dehydrogenase (ADHE) over the fluxes of fermentative glycolysis of Entamoeba histolytica subjected to aerobic conditions. The flux-control coefficients towards ethanol and acetate formation determined for PFOR titrated with diphenyleneiodonium were 0.07 and 0.09, whereas for ADHE titrated with disulfiram were 0.33 and −0.19, respectively. ADHE inhibition induced significant accumulation of glycolytic intermediates and lower ATP content. These results indicate that ADHE exerts significant flux-control on the carbon end-product formation of amoebas subjected to aerobic conditions.

Genetic modifications and introduction of heterologous pdc genes in Enterococcus faecalis for its use in production of bioethanol

Genetically-modified Enterococcus faecalis has a potential of survival and can be used in ethanolic fermentations. Fermentation profiles of E. faecalis JH2-2 were assessed using glucose and lactose as carbon sources. Deletion of lactate dehydrogenase (ldh) genes increased the ethanol production from 0.25 to 0.82 g/l, which was further increased to 0.96 g/l by the insertion of a pyruvate decarboxylase (pdc) gene (from Sarcina ventriculi or Clostridium acetobutylicum) in place ldh1. When grown on lactose, the pdcSv and pdcCa showed 13.6 and 17.6 U mg(-1) of pdc specific activity, respectively. Highest activity (47 U mg(-1)) and ethanol concentration (2.3 g/l) were obtained with pdcCa using an expression plasmid. Formate and acetate were also produced in high quantities. Transcriptional analysis showed that aldehyde alcohol dehydrogenase gene was upregulated up to 16-fold. Further optimizations are required for higher ethanol production.

Synthesis, Characterization and Biological Activity Studies of 1,3,4-Oxadiazole Analogs

The reaction of p-bromoanilino acetohydrazide(II) with aromatic aldehydes in alcohol yielded 2-[4-bromo aniline] N-substituted benzylidine hydrazides (IIIa-IIIj), which in presence of yellow mercuric oxide and iodine in DMF, yielded corresponding 4-bromo[(N-5-substituted 1,3,4 oxadiazole-2 –yl)methyl]aniline (IVa-IVj). Structures of the compounds synthesized were confirmed by IR, 1HNMR and MASS spectroscopic analysis. The newly synthesized compounds were screened for antibacterial, antifungal and anti-inflammatory activities. Some of the compounds showed remarkable antibacterial, antifungal and anti-inflammatory activities.

Microbial oxidases catalyzing conversion of glycolaldehyde into glyoxal

The present paper reviews oxidases catalyzing conversion of glycolaldehyde into glyoxal. The enzymatic oxidation of glycolaldehyde into glyoxal was first reported in alcohol oxidases (AODs) from methylotrophic yeasts such as Candida and Pichia, and glycerol oxidase (GLOD) from Aspergillus japonicus, although it had been reported that these enzymes are specific to short-chain linear aliphatic alcohols and glycerol, respectively. These enzymes continuously oxidized ethylene glycol into glyoxal via glycolaldehyde. The AODs produced by Aspergillus ochraceus and Penicillium purpurescens also oxidized glycolaldehyde. A new enzyme exhibiting oxidase activity for glycolaldehyde was reported from a newly isolated bacterium, Paenibacillus sp. AIU 311. The Paenibacillus enzyme exhibited high activity for aldehyde alcohols such as glycolaldehyde and glyceraldehyde, but not for methanol, ethanol, ethylene glycol or glycerol. The deduced amino acid sequence of the Paenibacillus AOD was similar to that of superoxide dismutases (SODs), but not to that of methylotrophic yeast AODs. Then, it was demonstrated that SODs had oxidase activity for aldehyde alcohols including glycolaldehyde. The present paper describes characteristics of glycolaldehyde oxidation by those enzymes produced by different microorganisms.

Study of a specific lignin model: γ-Oxidation and how it influences the hydrolysis efficiency of alcohol–aldehyde dehydrogenation copolymers

Six coniferyl alcohol–coniferaldehyde dehydrogenation copolymers (DHcoPs) were synthesized in order to determine the influence of an increased number of aldehyde functions on hydrolysis. After heterogeneous hydrolysis using acidic Montmorillonite K10 clay, the DHcoPs were thioacidolyzed and analyzed by gel permeation chromatography (GPC). Comparison of the thioacidolyzed products, with and without the hydrolysis step, showed that there was a greater proportion of condensation reaction in the absence of aldehyde. When the coniferaldehyde content in the initial synthetic mixture was more than 30% (w/w), only a low fraction of condensed products was generated during the K10 clay hydrolysis step. This suggests that condensation pathways are mainly due to the alcohol present in the γ-position in the DHcoPs. Investigation of the reactivity and the potential condensation of aldehyde and alcohol monomers under hydrolysis conditions showed the important conversion of coniferyl alcohol and conversely the stability of coniferaldehyde.

Pyruvate:ferredoxin oxidoreductase and bifunctional aldehyde–alcohol dehydrogenase are essential for energy metabolism under oxidative stress in Entamoeba histolytica

The in vitro Entamoeba histolytica pyruvate:ferredoxin oxidoreductase (EhPFOR) kinetic properties and the effect of oxidative stress on glycolytic pathway enzymes and fluxes in live trophozoites were evaluated. EhPFOR showed a strong preference for pyruvate as substrate over other oxoacids. The enzyme was irreversibly inactivated by a long period of saturating O(2) exposure (IC(50) 0.034 mm), whereas short-term exposure (< 30 min) leading to > 90% inhibition allowed for partial restoration by addition of Fe(2+). CoA and acetyl-CoA prevented, whereas pyruvate exacerbated, inactivation induced by short-term saturating O(2) exposure. Superoxide dismutase was more effective than catalase in preventing the inactivation, indicating that reactive oxygen species (ROS) were involved. Hydrogen peroxide caused inactivation in an Fe(2+)-reversible fashion that was not prevented by the coenzymes, suggesting different mechanisms of enzyme inactivation by ROS. Structural analysis on an EhPFOR 3D model suggested that the protection against ROS provided by coenzymes could be attributable to their proximity to the Fe-S clusters. After O(2) exposure, live parasites displayed decreased enzyme activities only for PFOR (90%) and aldehyde dehydrogenase (ALDH; 68%) of the bifunctional aldehyde-alcohol dehydrogenase (EhADH2), whereas acetyl-CoA synthetase remained unchanged, explaining the increased acetate and lowered ethanol fluxes. Remarkably, PFOR and ALDH activities were restored after return of the parasites to normoxic conditions, which correlated with higher ethanol and lower acetate fluxes. These results identified amebal PFOR and ALDH of EhADH2 activities as markers of oxidative stress, and outlined their relevance as significant controlling steps of energy metabolism in parasites subjected to oxidative stress.

Etherification of aldehydes, alcohols and their mixtures on Pd/SiO 2 catalysts

Dialkyl ethers have been selectively produced from etherification of aldehydes and alcohols on supported Pd catalysts. A yield of 79% ether with a selectivity of 90% was observed when feeding 2-methylpentanal with 2-methylpentanol at a molar ratio 1:1 at 125 °C. Cross etherification of n-butanol with 2-methylpentanal shows a much higher rate than that observed when the alcohol or aldehyde is fed alone. This enhanced activity is in line with the catalyst requirement for large ensembles that allow surface alkoxide species next to η 2 adsorbed aldehydes. Etherification when only aldehyde or alcohol is fed arises predominantly due to aldehyde–alcohol inter-conversion to produce the necessary co-reactant. The ether yield at the same reaction conditions decreases with metal loading in the order 16 > 10 > 3 wt.% Pd. Increasing reduction temperature also increases ether yield. It is apparent that etherification is highly sensitive to metal particle morphology, consistent with needing ensembles that accommodate the two adjacent adsorption sites.

Cloning, sequencing and expression analysis of a gene encoding alcohol oxidase in Paenibacillus sp. AIU 311

We have cloned a gene encoding an alcohol oxidase (AOD) specific to aldehyde alcohols from Paenibacillus sp. AIU 311. The AOD gene contains an open reading frame consisting of 618 nucleotides corresponding to 205 amino acid residues. The deduced amino acid sequence exhibits a high similarity to that of manganese superoxide dismutases (SODs). We expressed the cloned gene as an active product in Escherichia coli BL21 cells. The productivity (total units per culture broth volume) of the recombinant AOD expressed in E. coli BL21 is 26,000-fold higher than that of AOD in Paenibacillus sp. AIU 311. The recombinant AOD also exhibits aldehyde alcohol oxidase activity and SOD activity. The recombinant cells described in this study have utility for the production of glyoxal from glycolaldehyde.

ChemInform Abstract: Synthesis of Alkyl 2,5‐Dihydro‐5‐oxofuran‐2‐carboxylates via Palladium‐Catalyzed Carbonylative Cyclization of β‐Bromovinyl Aldehydes in Alcohols.

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Synthesis of alkyl 2,5-dihydro-5-oxofuran-2-carboxylates via palladium-catalyzed carbonylative cyclization of β-bromovinyl aldehydes in alcohols

β-Bromovinyl aldehydes reacts with carbon monoxide and alcohols at 125 °C in the presence of a catalytic amount of a palladium catalyst along with a base to give the corresponding carbonylative cyclized alkyl 2,5-dihydro-5-oxofuran-2-carboxylates in good yields. A reaction pathway involving intramolecular addition of acylpalladium to formyl group is proposed as a key step of this catalytic process.

Aldehyde–alcohol dehydrogenase and/or thiolase overexpression coupled with CoA transferase downregulation lead to higher alcohol titers and selectivity in Clostridium acetobutylicum fermentations

Metabolic engineering (ME) of Clostridium acetobutylicum has led to increased solvent (butanol, acetone, and ethanol) production and solvent tolerance, thus demonstrating that further efforts have the potential to create strains of industrial importance. With recently developed ME tools, it is now possible to combine genetic modifications and thus implement more advanced ME strategies. We have previously shown that antisense RNA (asRNA)-based downregulation of CoA transferase (CoAT, the first enzyme in the acetone-formation pathway) results in increased butanol to acetone selectivity, but overall reduced butanol yields and titers. In this study the alcohol/aldehyde dehydrogenase (aad) gene (encoding the bifunctional protein AAD responsible for butanol and ethanol production from butyryl-CoA and acetyl-CoA, respectively) was expressed from the phosphotransbutyrylase (ptb) promoter to enhance butanol formation and selectivity, while CoAT downregulation was used to minimize acetone production. This led to early production of high alcohol (butanol plus ethanol) titers, overall solvent titers of 30 g/L, and a higher alcohol/acetone ratio. Metabolic flux analysis revealed the likely depletion of butyryl-CoA. In order to increase then the flux towards butyryl-CoA, we examined the impact of thiolase (THL, thl) overexpression. THL converts acetyl-CoA to acetoacetyl-CoA, the first step of the pathway from acetyl-CoA to butyryl-CoA, and thus, combining thl overexpression with aad overexpression decreased, as expected, acetate and ethanol production while increasing acetone and butyrate formation. thl overexpression in strains with asRNA CoAT downregulation did not significantly alter product formation thus suggesting that a more complex metabolic engineering strategy is necessary to enhance the intracellular butyryl-CoA pool and reduce the acetyl-CoA pool in order to achieve improved butanol titers and selectivity.