Major aldehyde dehydrogenase AldFGH of Gluconacetobacter diazotrophicus is independent of pyrroloquinoline quinone but dependent on molybdopterin for acetic acid fermentation

2021 ◽  
Vol 105 (6) ◽  
pp. 2341-2350
Author(s):  
Roni Miah ◽  
Shun Nina ◽  
Takeru Murate ◽  
Naoya Kataoka ◽  
Minenosuke Matsutani ◽  
...  
2018 ◽  
Vol 102 (10) ◽  
pp. 4549-4561 ◽  
Author(s):  
Toshiharu Yakushi ◽  
Seiya Fukunari ◽  
Tomohiro Kodama ◽  
Minenosuke Matsutani ◽  
Shun Nina ◽  
...  

2010 ◽  
Vol 192 (21) ◽  
pp. 5718-5724 ◽  
Author(s):  
S. Gómez-Manzo ◽  
J. L. Chavez-Pacheco ◽  
M. Contreras-Zentella ◽  
M. E. Sosa-Torres ◽  
R. Arreguín-Espinosa ◽  
...  

ABSTRACT Several aldehyde dehydrogenase (ALDH) complexes have been purified from the membranes of acetic acid bacteria. The enzyme structures and the chemical nature of the prosthetic groups associated with these enzymes remain a matter of debate. We report here on the molecular and catalytic properties of the membrane-bound ALDH complex of the diazotrophic bacterium Gluconacetobacter diazotrophicus. The purified ALDH complex is a heterodimer comprising two subunits of 79.7 and 50 kDa, respectively. Reversed-phase high-pressure liquid chromatography (HPLC) and electron paramagnetic resonance spectroscopy led us to demonstrate, for the first time, the unequivocal presence of a pyrroloquinoline quinone prosthetic group associated with an ALDH complex from acetic acid bacteria. In addition, heme b was detected by UV-visible light (UV-Vis) spectroscopy and confirmed by reversed-phase HPLC. The smaller subunit bears three cytochromes c. Aliphatic aldehydes, but not formaldehyde, were suitable substrates. Using ferricyanide as an electron acceptor, the enzyme showed an optimum pH of 3.5 that shifted to pH 7.0 when phenazine methosulfate plus 2,6-dichlorophenolindophenol were the electron acceptors. Acetaldehyde did not reduce measurable levels of the cytochrome b and c centers; however, the dithionite-reduced hemes were conveniently oxidized by ubiquinone-1; this finding suggests that cytochrome b and the cytochromes c constitute an intramolecular redox sequence that delivers electrons to the membrane ubiquinone.


1987 ◽  
Vol 82 (8) ◽  
pp. 587-591
Author(s):  
Minoru AMEYAMA ◽  
Hiroki MATSUDA ◽  
Terumasa KUBOTA ◽  
Kouichi TAKIMOTO ◽  
Osao ADACHI

2011 ◽  
Vol 28 (6) ◽  
pp. 1175-1181 ◽  
Author(s):  
Wei Xu ◽  
Zhiyong Huang ◽  
Xiaojun Zhang ◽  
Qi Li ◽  
Zhenming Lu ◽  
...  

2014 ◽  
Vol 8 ◽  
pp. 161-168 ◽  
Author(s):  
Stella A. Ordoudi ◽  
Fani Mantzouridou ◽  
Eleni Daftsiou ◽  
Christine Malo ◽  
Efimia Hatzidimitriou ◽  
...  

Author(s):  
Yang Chen ◽  
Ye Bai ◽  
Dongsheng Li ◽  
Chao Wang ◽  
Ning Xu ◽  
...  

Abstract Acetic acid fermentation is an essential step in the production of high-quality fruit vinegar and typically involves the use of acetic acid bacteria (AAB). The present study showed that the high cell mass and acetic acid yields of ethanol-tolerant AAB under high ethanol conditions were related to the high activities and stability of both pyrroloquinoline quinone (PQQ)-dependent alcohol dehydrogenase and PQQ-dependent aldehyde dehydrogenase. Additionally, in acetic acid fermentation with watermelon wine (8 % ethanol), the main organic acids (acetic, tartaric and malic acids) produced by ethanol-tolerant Acetobacter pasteurianus AAB4 were higher than those by conventional A. pasteurianus AS1.41 (1.42-fold, 3.53-fold and 2.12-fold, respectively). Also, the main esters (ethyl acetate and phenylethyl acetate) produced by AAB4 were higher than those by AS1.41 (1.69-fold and 1.48-fold, respectively). In addition, the total sweet and umami free amino acids produced by AAB4 increased significantly. According to sensory analysis, the flavor, taste and overall acceptance score of watermelon vinegar produced by AAB4 were significantly higher than those by AS1.41. Therefore, high ethanol fermentation with ethanol-tolerant AAB improved the flavor and quality of watermelon vinegar, indicating that this technology can be applied to fruit vinegar production.


2019 ◽  
pp. 299-325
Author(s):  
Isidoro García-García ◽  
Jorge E. Jiménez-Hornero ◽  
Inés María Santos-Dueñas ◽  
Zoilo González-Granados ◽  
Ana María Cañete-Rodríguez

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