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PubMed2005

Induction of phenolsulfotransferase expression by phenolic acids in human hepatoma HepG2 cells.

Phenolic acids are antioxidant phenolic compounds, widespread in plant foods, which contribute significant biological and pharmacological properties; some have demonstrated a remarkable ability to alter sulfate conjugation. However, the modulation mechanisms of antioxidant phenolic acids on phenolsulfotransferase activity have not yet been described. In the present study, the human hepatoma cell line, HepG2, was used as a model to investigate the effect of antioxidant phenolic acids on enzymatic activity and expression of one of the major phase II sulfate conjugation enzymes, P-form phenolsulfotransferase (PST-P). The results showed that gallic acid, gentisic acid, p-hydroxybenzoic acid, and p-coumaric acid increased PST-P activity, in a dose-dependent manner. A maximum of 4- and 5-fold induction of PST-P activity was observed for both gallic acid and gentisic acid; however, they showed an adverse effect on cell growth at higher concentrations. A 2- or 2.5-fold increase of PST-P activity was found with either p-coumaric or p-hydroxybenzoic acid treatment, whereas no significant effect was found for ferulic acid treatment. PST-P induction, by gallic acid, was further confirmed, using reverse transcription PCR and Western blotting techniques to measure mRNA expression and protein translation. A significant correlation (r = 0.74, p < 0.01) between the expressions of PST-P mRNA and the corresponding PST-P activity was observed. Thus, gallic acid increased PST-P protein expression in HepG2 cells, in a dose- and time-dependent manner. The results demonstrated that certain antioxidant phenolic acids could induce PST-P activity in HepG2 cells, by promoting PST-P mRNA and protein expression, suggesting a novel mechanism by which phenolic acids may be implicated in phase II sulfate conjugation.

Arylsulfotransferase↗
PubMed2006

Crocin bleaching assay (CBA) in structure-radical scavenging activity studies of selected phenolic compounds.

The applicability of the crocin bleaching assay (CBA) to structure-activity relationship (SAR) studies of a great number (n = 39) of selected phenolic compounds was thoroughly investigated. The focus was on the activity of hydroxybenzoic, hydroxyphenylacetic, hydroxyphenylpropanoic, and hydroxycinnamic acids. Other assays [oxygen radical absorbance capacity (ORAC), lipid oxidation] were applied when necessary. Hydroxybenzoic acids were less active than the respective simple phenols. The position of the -COOH group relative to hydroxyl substituents was critical. The number and position of the -OH groups governed the order and size of activity within the subgroup of these acids. Gallic acid was the most active, being 1.6- and 3.4-fold superior to protocatechuic and syringic acids, respectively. The effect of proximity of the -COOH group to the phenyl ring was more distinct for 3,4-guaiacol acids (ferulic >> dihydroferulic congruent with homovanillic > vanillic) than for 3,4-catechol ones (caffeic >> protocatechuic > or = dihydrocaffeic congruent with homoprotocatechuic). Compounds such as vanillin, tyrosol, ferulic acid derivatives, rosmarinic acid, and quercetin were examined to reinforce discussion on the basis of physical organic chemistry principles. Taking into account the acidity of most compounds, the CBA-derived order of activity was meaningful.

Carotenoids↗
PubMed2000

Pathways for 3-chloro- and 4-chlorobenzoate degradation in Pseudomonas aeruginosa 3mT.

A bacterial isolate, Pseudomonas aeruginosa 3mT exhibited the ability to degrade high concentrations of 3-chlorobenzoate (3-CBA, 8 g l(-1)) and 4-chlorobenzoate (4-CBA 12 g l(-1)) (Ajithkumar 1998). In this study, by delineating the initial biochemical steps involved in the degradation of these compounds, we investigated how this strain can do so well. Resting cells, permeabilised cells as well as cell-free extracts failed to dechlorinate both 3-CBA and 4-CBA under anaerobic conditions, whereas the former two readily degraded both compounds under aerobic conditions. Accumulation of any intermediary metabolite was not observed during growth as well as reaction with resting cells under highly aerated conditions. However, on modification of reaction conditions, 3-chlorocatechol (3-CC) and 4-chlorocatechol (4-CC) accumulated in 3-CBA and 4-CBA flasks, respectively. Fairly high titres of pyrocatechase II (chlorocatechol 1,2-dioxygenase) activity were obtained in extracts of cells grown on 3-CBA and 4-CBA. Meta-pyrocatechase (catechol 2,3-dioxygenase) activity against 4-CC and catechol, but not against 3-CC, was also detected in low titres. Accumulation of small amounts of 2-chloro-5-hydroxy muconic semialdehyde, the meta-cleavage product of 4-CC, was detected in the medium, when 4-CBA concentration was 4 mM or greater, indicating the presence of a minor meta-pathway in strain 3mT. However, 3-CBA exclusively, and more than 99% of 4-CBA were degraded through the formation of the respective chlorocatechol, via a modified ortho-pathway. This defies the traditional view that the microbes that follow chlorocatechol pathways are not very good degraders of chlorobenzoates. 4-Hydroxybenzoate was readily (and 3-hydroxybenzoate to a lesser extent) degraded by the strain, through the formation of protocatechuate and gentisate, respectively, as intermediary dihydroxy metabolites.

2,2'-Dipyridyl↗
PubMed1998

Elevated "hydroxyl radical" generation in vivo in an animal model of amyotrophic lateral sclerosis.

Mutations in the enzyme copper/zinc superoxide dismutase-1 (SOD1) are associated with familial amyotrophic lateral sclerosis (FALS). The means by which the mutations cause FALS appears to be due to an adverse property of the mutant SOD1 protein that may involve increased generation of free radicals. We used in vivo microdialysis to measure the conversion of 4-hydroxybenzoic acid to 3,4-dihydroxybenzoic acid (3,4-DHBA) as a measure of "hydroxyl radical-like" production in transgenic amyotrophic lateral sclerosis (ALS) mice with the G93A mutation as well as littermate controls. The conversion of 4-hydroxybenzoic acid to 3,4-DHBA was significantly increased in the striatum of transgenic ALS mice at baseline but not in mice overexpressing wild-type human SOD1. Following administration of 3-nitropropionic acid 3,4-DHBA generation was significantly increased as compared with baseline, and the increase in the transgenic ALS mice was significantly greater than those in controls, whereas the increase in mice overexpressing wild-type human SOD1 was significantly attenuated. The present results provide in vivo evidence that expression of mutations in SOD1 can lead to increased generation of "hydroxyl radical-like" activity, which further implicates oxidative damage in the pathogenesis of ALS.

Amyotrophic Lateral Sclerosis↗
PubMed1998

Increased vulnerability to 3-nitropropionic acid in an animal model of Huntington's disease.

There is substantial evidence for both metabolic dysfunction and oxidative damage in Huntington's disease (HD). In the present study, we used in vivo microdialysis to measure the conversion of 4-hydroxybenzoic acid to 3,4-dihydroxybenzoic acid (3,4-DHBA) as a measure of hydroxyl radical production in a transgenic mouse model of HD, as well as in littermate controls. The conversion of 4-hydroxybenzoic acid to 3,4-DHBA was unchanged in the striatum of transgenic HD mice at baseline. Following administration of the mitochondrial toxin 3-nitropropionic acid (3-NP), there were significant increases in 3,4-DHBA generation in both control and transgenic HD mice, and the increases in the transgenic HD mice were significantly greater than those in controls. Furthermore, administration of 3-NP produced significantly larger striatal lesions in transgenic HD mice than in littermate controls. The present results show increased sensitivity to the mitochondrial toxin 3-NP in transgenic HD mice, which suggests metabolic dysfunction in this mouse model of HD.

Animals↗
PubMed2004

Protection capacity against low-density lipoprotein oxidation and antioxidant potential of some organic and non-organic wines.

Current research suggests that phenolics from wine may play a positive role against oxidation of low-density lipoprotein (LDL), which is a key step in the development of atherosclerosis. Considering the effects of different wine-making techniques on phenols and the wine consumption preference influencing the benefical effects of the product, organically and non-organically produced wines were obtained from the grapes of Vitis vinifera origin var: Carignan, Cabernet Sauvignon, Merlot, Grenache, Columbard and Semillon. Levels of total phenols [mg/l gallic acid equivalents (GAE)], antioxidant activity (%) and inhibition of LDL oxidation [%, inhibition of diene and malondialdehyde (MDA) formation] were determined. Some phenolic acids (gallic acid, p-hydroxybenzoic acid, syringic acid, 2,3-dihydroxybenzoic acid, ferulic acid, p-coumaric acid and vanillic acid) were quantified by high-performance liquid chromatography equipped with an electrochemical detection carried at +0.65 V (versus Ag/AgCl, 0.5 microA full scale). The highest concentrations of gallic, syringic and ferulic acids were found in organic Cabernet Sauvignon; 2,3-dihydroxybenzoic acid in organic Carignan and p-coumaric and vanillic acids in non-organic Merlot wine. High levels of antioxidant activity (AOA), inhibition of LDL oxidation and total phenol levels were found in non-organic Merlot (101.950% AOA; 88.570% LDL-diene; 41.000% LDL-MDA; 4700.000 mg/l GAE total phenol) and non-organic Cabernet Sauvignon (92.420% AOA; 91.430% LDL-diene; 67.000% LDL-MDA; 3500.000 mg/l GAE total phenol) grape varieties. Concentrations of some individual phenolic constituents (ferulic, p-coumaric, vanillic) are correlated with high antioxidant activity and inhibition of LDL oxidation. The best r value for all examined characteristics was determined for gallic acid, followed by 2,3-dihydroxybenzoic, syringic, ferulic and p-coumaric acids. Negative correlation of vanillic with MDA and p-hydroxybenzoic acid with LDL were confirmed by principal component analysis (PCA) analyses. Red wines display a higher antioxidant activity (81.110% AOA) than white ones (19.512% AOA). The average level of LDL inhibition capacity in red wine was determined as 87.072% and for the white as 54.867%.

Antioxidants↗
PubMed2003

Dietary compounds inhibit proliferation and contraction of keloid and hypertrophic scar-derived fibroblasts in vitro: therapeutic implication for excessive scarring.

BACKGROUND: Keloid and hypertrophic scars commonly occur after injuries. Overproliferation of fibroblasts, overproduction of collagen, and contraction characterize these pathologic scars. Current treatment of excessive scars with intralesional corticosteroid injections used individually or in combination with other methods often have unsatisfactory outcome, frustrating both the patient and the clinician. The phytochemical compounds are well known as potential anticancer agents. We have investigated the inhibitory effects of compounds on keloid fibroblasts (KF) and hypertrophic scar-derived fibroblasts (HSF). METHODS: Fibroblasts were cultured from nontreated earlobe keloids and burn hypertrophic scars. Ten compounds (three hydroxybenzoic and four hydroxycinnamic acid derivatives, two flavonols [quercetin and kaempferol], and turmeric curcumin) were tested with fibroblasts. The inhibitory effects of compounds on fibroblasts was assessed by proliferation assays, fibroblast-populated collagen lattice (FPCL) contraction, and electron microscopy. RESULTS: The phytochemicals significantly inhibited KF and HSF proliferation in a dose- and time-dependent manner. In the hydroxybenzoic and flavonol groups, increasing inhibitory effects seemed to depend on increasing numbers of hydroxyl groups in their chemical structures. This phenomenon was not observed in the hydroxycinnamic acid group. The phytochemicals inhibited fibroblast proliferation by inducing cell growth arrest but not apoptosis. The reversibility of growth inhibition occurred when the compounds were removed from the culture and fresh media was replaced. Slower reversibility of growth inhibition was observed in the groups treated with quercetin, chlorogenic acid, or curcumin. The compounds quercetin, gallic acid, protocatechuic acid, and chlorogenic acid were the strongest inhibitors of FPLC contraction by HTFs. When the compounds were washed out of the lattices and replaced by fresh medium, the FPCL contraction was resumed. The resumption of FPCL contraction was slowest in the quercetin-treated group, indicating again the strong inhibitory effect of quercetin. CONCLUSION: From this in vitro study, quercetin seemed to have good potent effects to inhibit proliferation and contraction of excessive scar-derived fibroblasts.

Adolescent↗
PubMed1984

On the biosynthesis of ubiquinones in plant mitochondria.

Isolated mitochondria from potato tubers, spinach leaves, and daffodil petals from intermediates of the ubiquinone biosynthetic pathway (prenylated 4-hydroxybenzoate, prenylated phenols, and quinoid compounds) from [1-14C]isopentenyl diphosphate and endogenous or exogenous 4-hydroxybenzoate. In contrast [2-14C]mevalonate 5-diphosphate, the immediate precursor of isopentenyl diphosphate was not accepted as a substrate. These results suggest that plant mitochondria have their own prenyltransferase and prenylation system, similar to the plastid compartment which also starts by the use of isopentenyl diphosphate [see Kreuz, K. and Kleinig, H. (1984) Eur. J. Biochem. 141, 531-535].

Cell Fractionation↗
PubMed2006

Biotransformation of p-coumaric acid by Paecilomyces variotii.

AIMS: To investigate the biotransformation of p-coumaric acid into p-hydroxybenzoic acid (p-HBA) by Paecilomyces variotii Bainier MTCC 6581. METHODS AND RESULTS: As a result of p-coumaric acid degradation by P. variotii, three phenolic metabolites, p-hydroxybenzaldehyde (p-HBAld), p-HBA and protocatechuic acid were formed. These phenolics were detected using TLC and HPLC. The identity of p-HBA and p-HBAld was further confirmed by mass spectrometry. Various analyses showed that 10.0 mmol l(-1) concentration of p-coumaric acid produced a maximum amount of p-hydroxybenzoic acid, 200 mg l(-1), into the medium at 37 degrees C with high-density cultures. CONCLUSIONS: A catabolic pathway of p-coumaric acid by the fungus P. variotii is suggested for the first time. During the process of p-coumaric acid degradation, p-HBA accumulated in the medium as the major degradation product. SIGNIFICANCE AND IMPACT OF THE STUDY: Microbial degradation of cinnamic acid and hydroxycinnamic acid has continued to be the focus of intensive study. The main goal was to identify the microbial species capable of converting these substances into commercially value-added products such as benzoic acid derivatives or aromatic aldehydes.

Benzaldehydes↗
PubMed1983

Salicylate and mitochondrial injury in Reye's syndrome.

Electron microscopic and spectrophotometric studies showed that salicylate causes gross swelling of mitochondria in isotonic salt solutions. In overall morphology the salicylate-treated mitochondria resembled those from patients with Reye's syndrome. Salicylate analogs such as m-hydroxybenzoate, p-hydroxybenzoate, and benzoate did not exert this effect. The mitochondria deformed by salicylate tended to return to their original condensed form on removal of the drug.

Animals↗
PubMed1982

Inhibition of Clostridium botulinum by antioxidants, phenols, and related compounds.

A total of 75 compounds, including antioxidants, preservatives, gallic acid and p-hydroxybenzoic acid esters, hydroquinones, hydroxyquinolines, phenol derivatives, and related compounds, were screened for their antibotulinal activity in prereduced Thiotone-yeast extract-glucose broth. The most effective inhibitors of Clostridium botulinum growth and toxin production were long-chain esters of p-hydroxybenzoic acid and gallic acid, antioxidants, and butylphenol derivatives. The antioxidant nordihydroguaiaretic acid at 100 microgram/ml delayed the growth and toxin production for the entire incubation period (7 days). Other antioxidants, such as butylated hydroxytoluene, butylated hydroxyanisole, and tert-butylhydroquinone were also very effective (at 200 to 400 microgram/ml) for the inhibition of C. botulinum growth and toxin production. Toxin was detected, although no detectable growth was found by daily absorbance measurements, in the prereduced medium containing 50 to 400 microgram of 8-hydroxyquinoline, pentylphenol, tert-pentylphenol, 3,5-ditert-butylphenol, 3,5-ditert-butylcatechol, (2-hydroxydiphenyl)methane, or (4-hydroxydiphenyl)methane per ml.

Antioxidants↗
PubMed1988

Anaerobic and aerobic metabolism of diverse aromatic compounds by the photosynthetic bacterium Rhodopseudomonas palustris.

The purple nonsulfur photosynthetic bacterium Rhodopseudomonas palustris used diverse aromatic compounds for growth under anaerobic and aerobic conditions. Many phenolic, dihydroxylated, and methoxylated aromatic acids, as well as aromatic aldehydes and hydroaromatic acids, supported growth of strain CGA001 in both the presence and absence of oxygen. Some compounds were metabolized under only aerobic or under only anaerobic conditions. Two other strains, CGC023 and CGD052, had similar anaerobic substrate utilization patterns, but CGD052 was able to use a slightly larger number of compounds for growth. These results show that R. palustris is far more versatile in terms of aromatic degradation than had been previously demonstrated. A mutant (CGA033) blocked in aerobic aromatic metabolism remained wild type with respect to anaerobic degradative abilities, indicating that separate metabolic pathways mediate aerobic and anaerobic breakdown of diverse aromatics. Another mutant (CGA047) was unable to grow anaerobically on either benzoate or 4-hydroxybenzoate, and these compounds accumulated in growth media when cells were grown on more complex aromatic compounds. This indicates that R. palustris has two major anaerobic routes for aromatic ring fission, one that passes through benzoate and one that passes through 4-hydroxybenzoate.

Aerobiosis↗
PubMed1994

Self-mobilization and organization of the genes encoding the toluene metabolic pathway of Pseudomonas mendocina KR1.

The toluene metabolic pathway of Pseudomonas mendocina KR1 is chromosomally encoded, but the pathway could be transferred by conjugation from strain KR1 to the chromosome of P. aeruginosa or P. putida. Such transconjugants utilized toluene, p-cresol, and p-hydroxybenzaldehyde. However, transconjugants were unable to further transfer toluene genes to other recipients unless Pseudomonas sex factor R68.45 was present in trans. Although the genes encoding the upper pathway for toluene metabolism in P. mendocina KR1 are sufficiently linked to permit their coordinate mobilization, they were found to be encoded in three independently regulated units: one encoding toluene-4-monooxygenase, a second encoding p-cresol methylhydroxylase and p-hydroxybenzaldehyde dehydrogenase, and a third encoding p-hydroxybenzoate hydroxylase. The last two regulatory units were cloned from the chromosome of a P. aeruginosa transconjugant onto a plasmid designated pRO1999. Analysis of pRO1999 showed that genes encoding p-cresol methylhydroxylase and p-hydroxybenzaldehyde dehydrogenase are organized as an operon; the gene encoding p-hydroxybenzaldehyde dehydrogenase is transcribed first, and this is followed by transcription of the gene encoding p-cresol methylhydroxylase. This operon is regulated by a positively acting regulator. The P. mendocina KR1 gene encoding p-hydroxybenzoate hydroxylase was linked to, but independently regulated from, the genes encoding toluene-4-monooxygenase, p-cresol methylhydroxylase, and p-hydroxybenzaldehyde dehydrogenase.

4-Hydroxybenzoate-3-Monooxygenase↗
PubMed1965

EFFECT OF PHENOLIC ACIDS AND ESTERS ON RESPIRATION AND REPRODUCTION OF BACTERIA IN URINE.

Vanillic, syringic, gallic, and protocatechuic acids, methyl-p-hydroxybenzoate, and propyl-p-hydroxybenzoate generally inhibited respiration in vitro of Escherichia coli, Proteus vulgaris, Pseudomonas aeruginosa, and Aerobacter aerogenes in human urine. In the absence of any other available carbon source, certain of the phenolic compounds were utilized. Reproduction was generally suppressed in urine buffered to pH 7, 5.6, 4.5, and 4.0. The phenolic compounds were used in the range of 0.11 to 0.99 mumole/ml.

Bacteria↗
PubMed1976

Constitutive synthesis of enzymes of the protocatechuate pathway and of the beta-ketoadipate uptake system in mutant strains of Pseudomonas putida.

Mutant Pseudomonas putida strains that produce constitutive levels of the beta-ketoadipate uptake system are selected by the sequential transfer of cultures between mineral growth media supplemented with the noninducing growth substrate succinate and growth media containing beta-ketoadipate as the sole carbon and energy source. The mutant strains also produce constitutively three catabolic enzymes that give rise to beta-ketoadipate from the metabolic precursor beta-carboxy-cis, cis-muconate, and thus a single regulatory gene appears to govern the expression of the enzymes as well as the uptake system. The three enzymes that convert beta-carboxy-cis, cis-muconate to beta-ketoadipate are induced to higher levels when the orgainisms are grown with p-hydroxybenzoate (a compound that is catabolized via beta-ketoadipate); the beta-ketoadipate uptake system is partially repressed when the cells are grwon at the expense of p-hydroxybenzoate. The transferase that acts upon beta-ketoadipate remains inducible in the constitutive mutant strains. Thus a minimum of three biosynthetic controls must be exerted over the expression of the five genes. Since the regulatory mutation does not alter the expression of the gene for the transferase, the physiological target of the selection procedure appears to be mutant strains that produce the uptake system constitutively. Levels of the uptake system are higher in uninduced constitutive mutant cultures than in induced cultures of the wild type. Hence procedures analogous to the one we employed may be of general use in obtaining mutant strains that produce high levels of uptake systems.

Adipates↗
PubMed1979

Catabolism of L-tyrosine in Trichosporon cutaneum.

Protocatechuic acid was a catabolite in the degradation of L-tyrosine by Trichosporon cutaneum. Intact cells oxidized to completion various compounds proposed as intermediates in this conversion, but they did not readily oxidize catabolites of the homogentisate and homoprotocatechuate metabolic pathways, which are known to function in other organisms. Cell extracts converted tyrosine first to 4-hydroxycinnamic acid and then to 4-hydroxybenzaldehyde and 4-hydroxybenzoic acid. The proposed hydration product of 4-hydroxycinnamic acid, namely, beta-(4-hydroxyphenyl)-hydracrylic acid, was synthesized chemically, and its enzymatic degradation to 4-hydroxybenzaldehyde was shown to be dependent upon additions of adenosine triphosphate and coenzyme A. The hydroxylase that attacked 4-hydroxybenzoate showed a specific requirement for reduced nicotinamide adenine dinucleotide phosphate. Protocatechuate, the product of this reaction, was oxidized by cell extracts supplemented with reduced nicotinamide adenine dinucleotide or, less effectively, with reduced nicotinamide adenine dinucleotide phosphate, but these extracts contained no ring fission dioxygenase for protocatechuate. Evidence is presented that the principal hydroxylation product of protocatechuate was hydroxyquinol, the benzene nucleus of which was cleaved oxidatively to give maleylacetic acid.

Coumaric Acids↗
PubMed1980

Regulation of enzymes of the 3,5-xylenol-degradative pathway in Pseudomonas putida: evidence for a plasmid.

Constitutive synthesis of enzymes responsible for methyl group oxidation in 3,5-xylenol degradation and an associated p-cresol methylhydroxylase in Pseudomonas putida NCIB 9869 was shown by their retention at high specific activities in cells transferred from 3,5-xylenol medium to glutamate medium. The specific activities of other enzymes of the 3,5-xylenol pathway declined upon removal of aromatic substrate, consistent with their inducible control. Specific activities of the methyl-oxidizing enzymes showed an eventual decline concomitant with a decrease in the fraction of bacteria capable of growth with 3,5-xylenol; a simultaneous loss of the ability to grow with m-hydroxybenzoate was also observed. The property of 3,5-xylenol utilization could be transferred to another strain of P. putida. It is proposed that enzymes of the 3,5-xylenol pathway and those for conversion of p-cresol to p-hydroxybenzoate are plasmid encoded, that the early methyl-oxidizing enzymes are expressed constitutively, and that the later enzymes are inducible.

Alcohol Oxidoreductases↗
PubMed1990

Biotransformations of carboxylated aromatic compounds by the acetogen Clostridium thermoaceticum: generation of growth-supportive CO2 equivalents under CO2-limited conditions.

Clostridium thermoaceticum ATCC 39073 converted vanillate to catechol. Although carboxylated aromatic compounds which did not contain methoxyl groups were not by themselves growth supportive, protocatechuate and p-hydroxybenzoate (nonmethoxylated aromatic compounds) were converted to catechol and phenol, respectively, during carbon monoxide-dependent growth. Syringate is not subject to decarboxylation by C. thermoaceticum (Z. Wu, S. L. Daniel, and H. L. Drake, J. Bacteriol. 170:5705-5708, 1988), and sustained growth at the expense of syringate-derived methoxyl groups was dependent on supplemental CO2. In contrast, vanillate was growth supportive in the absence of supplemental CO2, and 14CO2 was the major 14C-labeled product during [carboxyl-14C]vanillate-dependent growth. Furthermore, the decarboxylation of protocatechuate and p-hydroxybenzoate supported methanol- and 1,2,3-trimethoxybenzene-dependent growth (CO2 is required for growth at the expense of these substrates) when supplemental CO2 was depleted from the growth medium, and the decarboxylation of protocatechuate was concomitant with improved cell yields of methanol cultures. These findings demonstrate that (i) C. thermoaceticum is competent in the decarboxylation of certain aromatic compounds and (ii) under certain conditions, decarboxylation may be integrated to the flow of carbon and energy during acetogenesis.

Biotransformation↗