A Novel Type of Formaldehyde-Oxidizing Enzyme from the Membrane of<i>Acetobacter</i>sp. SKU 14

Shinagawa, Emiko; Toyama, Hirohide; Matsushita, Kazunobu; Tuitemwong, Pravate; Theeragool, Gunjana; Adachi, Osao

doi:10.1271/bbb.70.850

Cited by 18 publications

(9 citation statements)

References 24 publications

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“…Interestingly, it was previously reported that the ADH-III of G. polyoxogenes (formerly Acetobacter polyoxogenes [ 15 ], Ga. xylinus [ 16 ], Acetobacter sp. SKU 14 [ 17 ], Ga. diazotrophiocus [ 18 ] and Acetobacter pasteurianus MSU10 [ 19 ], showed significant activity on formaldehyde and acetaldehyde, respectively.…”

Section: Discussionmentioning

confidence: 99%

“…However, it has been reported that in some species as G. polyoxogenes (formerly Acetobacter polyoxogenes [ 15 ], Ga. xylinus [ 16 ], Acetobacter sp. SKU 14 [ 17 ], Ga. diazotrophiocus [ 18 ] and Acetobacter pasteurianus MSU10 [ 19 ], ADH enzymes exhibited activity, also with formaldehyde and acetaldehyde. In previous studies Gomez-Manzo et al [ 18 , 20 ] purified and characterized two types of Class III ADHs from Ga. diazotrophicus : ADH active (ADHa) and the inactive (ADHi).…”

Section: Introductionmentioning

confidence: 99%

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The Oxidative Fermentation of Ethanol in Gluconacetobacter diazotrophicus Is a Two-Step Pathway Catalyzed by a Single Enzyme: Alcohol-Aldehyde Dehydrogenase (ADHa)

Gómez-Manzo

Escamilla

González‐Valdez

et al. 2015

IJMS

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Gluconacetobacter diazotrophicus is a N2-fixing bacterium endophyte from sugar cane. The oxidation of ethanol to acetic acid of this organism takes place in the periplasmic space, and this reaction is catalyzed by two membrane-bound enzymes complexes: the alcohol dehydrogenase (ADH) and the aldehyde dehydrogenase (ALDH). We present strong evidence showing that the well-known membrane-bound Alcohol dehydrogenase (ADHa) of Ga. diazotrophicus is indeed a double function enzyme, which is able to use primary alcohols (C2–C6) and its respective aldehydes as alternate substrates. Moreover, the enzyme utilizes ethanol as a substrate in a reaction mechanism where this is subjected to a two-step oxidation process to produce acetic acid without releasing the acetaldehyde intermediary to the media. Moreover, we propose a mechanism that, under physiological conditions, might permit a massive conversion of ethanol to acetic acid, as usually occurs in the acetic acid bacteria, but without the transient accumulation of the highly toxic acetaldehyde.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The Oxidative Fermentation of Ethanol in Gluconacetobacter diazotrophicus Is a Two-Step Pathway Catalyzed by a Single Enzyme: Alcohol-Aldehyde Dehydrogenase (ADHa)

Gómez-Manzo

Escamilla

González‐Valdez

et al. 2015

IJMS

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“…The substrate specificity of AAB mADH usually is very poor. Except for methanol, short-chain alcohols such as ethanol, 1-propanol, 1-butanol, 1-pentanol, and 1-hexanol can be utilized as its substrates (Shinagawa et al, 2006 ). In addition, mADH can also produce glyceraldehyde from glycerol, although it only has a low affinity for glycerol.…”

Section: Aab Oxidative Fermentationmentioning

confidence: 99%

“…Therefore, mADH alone can carry out the entire oxidation process from ethanol to acetaldehyde to acetic acid without the involvement of membrane-binding acetaldehyde dehydrogenase (mALDH) [EC 1.2.1.10] (Gómez-Manzo et al, 2015 ). In addition, although mADH cannot oxidize methanol, it can oxidize formaldehyde so that mADH can be developed as a formaldehyde scavenger (Shinagawa et al, 2006 ).…”

Section: Aab Oxidative Fermentationmentioning

confidence: 99%

Oxidative Fermentation of Acetic Acid Bacteria and Its Products

Xie

Zhang

et al. 2022

Front. Microbiol.

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Acetic acid bacteria (AAB) are a group of Gram-negative, strictly aerobic bacteria, including 19 reported genera until 2021, which are widely found on the surface of flowers and fruits, or in traditionally fermented products. Many AAB strains have the great abilities to incompletely oxidize a large variety of carbohydrates, alcohols and related compounds to the corresponding products mainly including acetic acid, gluconic acid, gulonic acid, galactonic acid, sorbose, dihydroxyacetone and miglitol via the membrane-binding dehydrogenases, which is termed as AAB oxidative fermentation (AOF). Up to now, at least 86 AOF products have been reported in the literatures, but no any monograph or review of them has been published. In this review, at first, we briefly introduce the classification progress of AAB due to the rapid changes of AAB classification in recent years, then systematically describe the enzymes involved in AOF and classify the AOF products. Finally, we summarize the application of molecular biology technologies in AOF researches.

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“…Microbial methods have attracted increasing attention because of their feasibility and rapid decontamination. Numerous microorganisms tolerant to formaldehyde have been isolated and characterized, including Methylobacterium[26], Pseudomonas [27,28], Rhodococcus [29], Bacillus [30], Aspergillus [31], Paecilomyces [32], microalgae Nannochloropsis oculata [33], Acetobacter [34] and Corynebacterium glutamicum [35]. Among these reported strains, those belonging to Pseudomonas sp.…”

Section: Introductionmentioning

confidence: 99%

Random mutagenesis of a Pseudomonas putida strain capable of acclimating to high-concentration formaldehyde via atmospheric and room temperature plasma(ARTP)

Kong

2022

Preprint

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Formaldehyde has strong cytotoxicity to organisms and may cause nasopharyngeal cancer and probably leukemia. This study is intended to investigate a highly formaldehyde-resistant utilizer, the Pseudomonas putida W1 strain. Bacterial strain W1 isolated from untreated activated sludge samples collected from heavily formaldehyde- and aniline-contaminated areas was identified using morphological characteristics and molecular techniques. The formaldehyde concentration in the medium decreased with the growth of strain W1. The degradation of formaldehyde concentration depends on the cell number of strain W1. The W1 strain completely consumed 0.5 g L-1 of nearly 98% formaldehyde within 48 h. Atmospheric and room temperature plasma (ARTP) was applied to improve the tolerance to formaldehyde and the genetic stability of P. putida. The protocol for rapid mutation was established by different intervals with a fatality rate reaching 99% and then compared with the dual gradient plate screening method. Growth of the isolated mutant WMZ120-5 strain on formaldehyde was possible up to at least 3 g L-1, and survival at up to a concentration of 20 g L-1 was possible after stepwise acclimatization. At such high concentrations of formaldehyde, the mutant WMZ120-5 exhibited approximately seven-fold higher expression than the original strain W1. The characteristics of the mutant after mutagenesis showed good genetic stability after the 10th subculture. Our study demonstrated that strain WMZ120-5 has great potential to utilize formaldehyde at high concentrations in the environment.

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A Novel Type of Formaldehyde-Oxidizing Enzyme from the Membrane ofAcetobactersp. SKU 14

Cited by 18 publications

References 24 publications

The Oxidative Fermentation of Ethanol in Gluconacetobacter diazotrophicus Is a Two-Step Pathway Catalyzed by a Single Enzyme: Alcohol-Aldehyde Dehydrogenase (ADHa)

The Oxidative Fermentation of Ethanol in Gluconacetobacter diazotrophicus Is a Two-Step Pathway Catalyzed by a Single Enzyme: Alcohol-Aldehyde Dehydrogenase (ADHa)

Oxidative Fermentation of Acetic Acid Bacteria and Its Products

Random mutagenesis of a Pseudomonas putida strain capable of acclimating to high-concentration formaldehyde via atmospheric and room temperature plasma(ARTP)

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