Spore-forming bacteria that carboxylate phenol to benzoic acid under anaerobic conditions

1995 ◽  
Vol 41 (3) ◽  
pp. 266-272 ◽  
Author(s):  
L. Létouraeau ◽  
J.-G. Bisaillon ◽  
F. Lépine ◽  
R. Beaudet
Keyword(s):  
Benzoic Acid ◽  
Solid Medium ◽  
Hydroxybenzoic Acid ◽  
Strictly Anaerobic ◽  
Anaerobic Conditions ◽  
Electron Microscopic ◽  
Untreated Culture ◽  
Spore Forming Bacteria ◽  
Hydroxybenzyl Alcohol ◽  
Methanogenic Consortium

A methanogenic consortium transforming phenol to benzoic acid was submitted to different treatments to characterize the carboxylating microorganisms and eventually to facilitate their isolation. Under aerobic conditions, phenol was not transformed by the consortium and no growth was observed on solid medium. The consortium from an inoculum that was treated with heat, or heat and ethanol, retained the ability to carboxylate phenol under strictly anaerobic conditions. Electron microscopic observations of the consortium from an inoculum that was heated for 15 min at 80 °C revealed only Gram-positive bacilli. In this culture, methane production was not detected and benzoic acid accumulated. Five colonies with distinct morphologies were isolated from this culture on solid medium. Four of these strains were identified as Clostridium spp. In contrast to the untreated culture, none of the strains isolated were able to carboxylate phenol in pure culture or in coculture, nor could they decarboxylate or dehydroxylate 4-hydroxybenzoic acid, or oxidize 2-hydroxybenzyl alcohol, or O-demethylate anisole or 2-methoxyphenol. Also, the consortium from a treated inoculum retained its ability to decarboxylate and dehydroxylate 4-hydroxybenzoic acid forming phenol and benzoic acid, respectively, but could not accomplish the other reactions. These results suggest that spore-forming microorganisms are involved in the carboxylation of phenol and in the decarboxylation and dehydroxylation of 4-hydroxybenzoic acid.Key words: spore-forming bacteria, phenol, benzoic acid, methanogenic conditions, carboxylation.

Potential for carboxylation–dehydroxylation of phenolic compounds by a methanogenic consortium

1993 ◽  
Vol 39 (7) ◽  
pp. 642-648 ◽  
Author(s):  
Jean-Guy Bisaillon ◽  
François Lépine ◽  
Réjean Beaudet ◽  
Michel Sylvestre
Keyword(s):  
Phenolic Compounds ◽  
Hydroxybenzoic Acid ◽  
Benzoic Acids ◽  
Substituted Phenols ◽  
Proteose Peptone ◽  
Anaerobic Consortium ◽  
Transformation Activity ◽  
Substituted Benzoic Acids ◽  
Hydroxybenzyl Alcohol ◽  
Methanogenic Consortium

An anaerobic consortium that carboxylated and dehydroxylated phenol to benzoate, and 2-cresol to 3-methylbenzoic acid, under methanogenic conditions was studied. Phenol induced this transformation activity. Addition of 4-hydroxypyridine or an increase in the concentration of proteose peptone to 0.5% (w/v) delayed the transformation. Phenol enhanced the rate of transformation of 2-cresol whereas 2-cresol delayed the transformation of phenol. Phenols with ortho-substitutions (chloro-, fluoro-, bromo-, hydroxyl-, amino-, or carboxyl-) were transformed to meta-substituted benzoic acids. However, meta- and para-substituted phenols (cresols, fluorophenols, and chlorophenols) were not transformed. Phenol was most rapidly metabolized, followed by catechol, 2-cresol, 2-fluorophenol, 2-aminophenol, 2-chlorophenol, 2-hydroxybenzoic acid, and 2-bromophenol. The consortium O-demethylated anisole to phenol and 2-methoxyphenol to catechol, and oxidized 2-hydroxybenzyl alcohol to 2-hydroxybenzoic acid. Aniline, 2-ethylphenol, 2-hydroxypyridine, 2-acetamidophenol, 2,6-dimethylphenol, 2-phenylphenol, and 1-naphthol were not metabolized.Key words: phenolic compounds, methanogenic consortium, carboxylation–dehydroxylation.

Formation of Benzoic Acid and p-Hydroxybenzoic Acid in the Blue Green Alga Anacystis nidulans: A Thylakoid-Bound Enzyme Complex Analogous to the Chloroplast System

1976 ◽  
Vol 31 (11-12) ◽  
pp. 693-699 ◽  
Author(s):  
W. Löffelhardt ◽  
H. Kindl
Keyword(s):  
Benzoic Acid ◽  
Phenylalanine Ammonia Lyase ◽  
Higher Plants ◽  
Anacystis Nidulans ◽  
Striking Similarity ◽  
Hydroxybenzoic Acid ◽  
Cinnamic Acids ◽  
Tyrosine Ammonia Lyase ◽  
Membrane Bound ◽  
Enzyme Complexes

Abstract Membrane-Bound Enzyme Complexes, Anacystis nidulans, Thylakoids, Benzoate Synthase The photosynthetic procaryote Anacystis nidulans converts L-phenylalanine and L-tyrosine into benzoic acid and p-hydroxybenzoic acid, respectively. Results obtained with thylakoid fractions support the hypothesis that the reaction sequence is catalyzed by thylakoid-bound enzyme complexes consisting of phenylalanine ammonia-lyase and benzoate synthase or tyrosine ammonia-lyase and p-hydroxybenzoate synthase, respectively. Both complexes do not accept phenylacetic acids as substrates, and cinnamic acids only at a small extent. These properties suggest a striking similarity to a benzoic acid-synthesizing enzyme system from higher plants which is situated at the thylakoid membrane of chloroplasts. The respective complexes of Dunaliella marina and Porphyridium sp. were included in this comparison.

scholarly journals CO2 Improved Synthesis of Benzimidazole with the Catalysis of a New Calcium 4-Amino-3-hydroxybenzoate

2021 ◽  
Vol 68 (1) ◽  
pp. 205-211
Author(s):  
Ruo-Xuan Gao ◽  
Yuan-Yuan Gao ◽  
Ning Zhu ◽  
Li-Min Han
Keyword(s):  
Synergistic Effect ◽  
Benzoic Acid ◽  
Calcium Salt ◽  
Tricarboxylic Acid ◽  
Hydroxybenzoic Acid ◽  
Catalyst Screening

In this paper, we explored the synthesis of benzimidazole by the reaction of DMF and o-phenylenediamine. In the process of catalyst screening, we found that 4-amino-3-hydroxybenzoic acid, benzoic acid, and benzene-1,3,5-tricarboxylic acid could catalyze the reaction. Moreover, the calcium 4-amino-3-hydroxybenzoate and CO2 could more effectively catalyze the reaction, the synergistic effect of CO2 and 4-amino-3-hydroxybenzoic acid calcium salt can increase the yield of benzimidazole from 28% to 94%.

Versatile Cryostated Optically Transparent Thin-Layer Electrochemical (OTTLE) Cell for Variable-Temperature UV-Vis/IR Spectroelectrochemical Studies

1994 ◽  
Vol 48 (12) ◽  
pp. 1522-1528 ◽  
Author(s):  
F. Hartl ◽  
H. Luyten ◽  
H. A. Nieuwenhuis ◽  
G. C. Schoemaker
Keyword(s):  
Thin Layer ◽  
Low Temperatures ◽  
Variable Temperature ◽  
Experimental Setup ◽  
Strictly Anaerobic ◽  
Carbonyl Complexes ◽  
Anaerobic Conditions ◽  
Optically Transparent ◽  
Solution Layer ◽  
Preset Temperature

This article describes the construction of a novel optically transparent thin-layer electrochemical (OTTLE) cell for IR and UV-Vis spectroelectrochemical experiments at variable temperature. The cell has a three-electrode set melt-sealed into a smooth polyethylene spacer which is sandwiched between two CaF2 windows. The width of this spacer (0.18–0.20 mm) defines the thickness of the thin solution layer. The whole electrode assembly is housed in a thermostated Cu block of the OTTLE cell which fits into a double-walled nitrogen-bath cryostat. The experimental setup permits relatively fast electrolysis within the tested temperature range of 295 to 173 K under strictly anaerobic conditions and protection of light-sensitive compounds. Other important merits of the cell design include lack of leakage, facile cleaning, almost negligible variation of the preset temperature, and facile manipulation in the course of the experiments. The applicability of the variable-temperature IR/UV-Vis OTTLE cell is demonstrated by stabilization of a few electrogenerated carbonyl complexes of Mn(I) and Ru(II) with 3,5-di- tert. butyl-1,2-benzo(semi)quinone (DB(S)Q) and N, N′-diisopropyl-1,4-diaza-1,3-butadiene (iPr-DAB) ligands, respectively, at appropriately low temperatures.

scholarly journals Redesigning Escherichia coli Metabolism for Anaerobic Production of Isobutanol

2011 ◽  
Vol 77 (14) ◽  
pp. 4894-4904 ◽  
Author(s):  
Cong T. Trinh ◽  
Johnny Li ◽  
Harvey W. Blanch ◽  
Douglas S. Clark
Keyword(s):  
Escherichia Coli ◽  
Anaerobic Growth ◽  
Mode Analysis ◽  
Glycolytic Flux ◽  
Strictly Anaerobic ◽  
Anaerobic Conditions ◽  
Content Type ◽  
E Coli ◽  
Model Predictions ◽  
Chromosomal Genes

ABSTRACTFermentation enables the production of reduced metabolites, such as the biofuels ethanol and butanol, from fermentable sugars. This work demonstrates a general approach for designing and constructing a production host that uses a heterologous pathway as an obligately fermentative pathway to produce reduced metabolites, specifically, the biofuel isobutanol. Elementary mode analysis was applied to design anEscherichia colistrain optimized for isobutanol production under strictly anaerobic conditions. The central metabolism ofE. coliwas decomposed into 38,219 functional, unique, and elementary modes (EMs). The model predictions revealed that during anaerobic growthE. colicannot produce isobutanol as the sole fermentative product. By deleting 7 chromosomal genes, the total 38,219 EMs were constrained to 12 EMs, 6 of which can produce high yields of isobutanol in a range from 0.29 to 0.41 g isobutanol/g glucose under anaerobic conditions. The remaining 6 EMs rely primarily on the pyruvate dehydrogenase enzyme complex (PDHC) and are typically inhibited under anaerobic conditions. The redesignedE. colistrain was constrained to employ the anaerobic isobutanol pathways through deletion of 7 chromosomal genes, addition of 2 heterologous genes, and overexpression of 5 genes. Here we present the design, construction, and characterization of an isobutanol-producingE. colistrain to illustrate the approach. The model predictions are evaluated in relation to experimental data and strategies proposed to improve anaerobic isobutanol production. We also show that the endogenous alcohol/aldehyde dehydrogenase AdhE is the key enzyme responsible for the production of isobutanol and ethanol under anaerobic conditions. The glycolytic flux can be controlled to regulate the ratio of isobutanol to ethanol production.

Histochemical Demonstration of Certain DPN-Linked Dehydrogenases and of Aldolase in the Red and White Fibres of Pigeon Breast-Muscle

1962 ◽  
Vol s3-103 (61) ◽  
pp. 41-46
Author(s):  
J. C. GEORGE ◽  
C. L. TALESARA
Keyword(s):  
Enzyme Activity ◽  
Histochemical Demonstration ◽  
Breast Muscle ◽  
Strictly Anaerobic ◽  
Anaerobic Conditions ◽  
High Concentration ◽  
Hydrogen Acceptor ◽  
Localization Pattern ◽  
Important Link

The distribution and localization-pattern of certain DPN-linked dehydrogenases (malic, lactic, D-glucose, glutamic, and a-glycerophosphate) were demonstrated histochemically in the red and white fibres of pigeon breast-muscle by using neotetrazolium as the hydrogen acceptor, under strictly anaerobic conditions. All the dehydrogenases studied showed distinctly higher enzyme activity in the narrow red fibres than in the broad white fibres. That of a-glycerophosphate was, however, found to be appreciably more abundant than other dehydrogenases in the broad fibres. A high concentration of aldolase, which forms an important link in the chain of enzymes in glycolysis, was histochemically demonstrated in the broad, white, glycogen-loaded fibres.

scholarly journals Myothermic apparatus

1928 ◽  
Vol 103 (723) ◽  
pp. 117-137 ◽  
Keyword(s):  
Heat Production ◽  
Present Author ◽  
Single Stimulus ◽  
Relative Accuracy ◽  
Strictly Anaerobic ◽  
Anaerobic Conditions ◽  
Essential Condition ◽  
Energy Exchanges

The investigation to be described in subsequent papers represent an attempt to clear up, with the greatest accuracy possible, a number of outstanding or controversial points in connection with the energy exchanges of muscle. During the course of them a new and striking phenomenon has been encountered, in respect of the resting heat-production of muscles kept under strictly anaerobic conditions. It has been necessary, moreover, for various purposes, to follow the heat-production of stimulated or recovering muscles for long periods, sometimes for an hour or more. The apparatus available proved inadequate for these new purposes, and had to be designed and constructed afresh. The present paper is a description of the methods finally adopted; the results obtained are given separately. In almost every respect the apparatus now employed will yield more reliable results, and is simpler to use, than any previously described, at any rate by the present author. The essential condition which it fulfils is that it will read, with relative accuracy, not only the heat suddenly produced by a single stimulus, but that liberated over long intervals at rest, or in recovery, or by prolonged discontinuous stimulation.

Synergistic staphylocidal interaction of benzoic acid derivatives (benzoic acid, 4-hydroxybenzoic acid and β-resorcylic acid) and capric acid: mechanism and verification study using artificial skin

2019 ◽  
Vol 75 (3) ◽  
pp. 571-575
Author(s):  
H W Kim ◽  
Y S Seok ◽  
M S Rhee
Keyword(s):  
Benzoic Acid ◽  
Synergistic Effects ◽  
Capric Acid ◽  
Pharmaceutical Products ◽  
Artificial Skin ◽  
Membrane Disruption ◽  
Hydroxybenzoic Acid ◽  
Benzoic Acid Derivatives ◽  
Log Reduction ◽  
Ion Imbalance

Abstract Objectives The present study was designed to investigate a synergistic staphylocidal interaction of antimicrobials. Methods The widely used preservative benzoic acid (BzA) and its derivatives [4-hydroxybenzoic acid (HA) and β-resorcylic acid (β-RA)] combined with capric acid (CPA) were investigated. Results β-RA was identified as the most effective antimicrobial exhibiting synergistic action with CPA against both Staphylococcus aureus and MRSA. For example, a complete reduction of bacteria (>7.3 log reduction) was obtained within 5 min after treatment with 5.0 mM β-RA (0.079%) plus 0.20 mM CPA (0.004%), while treatment with each material individually showed low bactericidal effects (<1.5 log reduction). Flow cytometry analysis identified membrane disruption related to the synergistic mechanisms, including the following: (i) membrane disruption by CPA (69.2% of cells were damaged by 0.20 mM CPA treatment); (ii) antimicrobial entry through the damaged membrane; and (iii) cytoplasmic ion imbalance resulting in cell death. We verified that the synergistic combination was also effective against MRSA on artificial skin (99.989% elimination after 5 min). Conclusions We used only consumer-preferred natural-borne antimicrobials and a very small amount of material was needed based on the synergistic effects. Therefore, these antimicrobials can be widely used as alternative anti-MRSA compounds in healthcare products, cosmetics, pharmaceutical products, foods and for environmental hygiene.

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