scholarly journals Formation of 4-Keto-D-aldopentoses and 4-Pentulosonates (4-Keto-D-pentonates) with Unidentified Membrane-Bound Enzymes from Acetic Acid Bacteria

2011 ◽  
Vol 75 (9) ◽  
pp. 1801-1806 ◽  
Author(s):  
Osao ADACHI ◽  
Roque A. HOURS ◽  
Emiko SHINAGAWA ◽  
Yoshihiko AKAKABE ◽  
Toshiharu YAKUSHI ◽  
...  
Keyword(s):  
Acetic Acid ◽  
Acetic Acid Bacteria ◽  
Membrane Bound ◽  
Membrane Bound Enzymes

Identifying membrane-bound quinoprotein glucose dehydrogenase from acetic acid bacteria that produce lactobionic and cellobionic acids

2019 ◽  
Vol 83 (6) ◽  
pp. 1171-1179 ◽  
Author(s):  
Takaaki Kiryu ◽  
Taro Kiso ◽  
Daisuke Koma ◽  
Shigemitsu Tanaka ◽  
Hiromi Murakami
Keyword(s):  
Acetic Acid ◽  
Glucose Dehydrogenase ◽  
Acetic Acid Bacteria ◽  
Membrane Bound

scholarly journals A tunable l-arabinose-inducible expression plasmid for the acetic acid bacterium Gluconobacter oxydans

2020 ◽  
Vol 104 (21) ◽  
pp. 9267-9282
Author(s):  
Philipp Moritz Fricke ◽  
Tobias Link ◽  
Jochem Gätgens ◽  
Christiane Sonntag ◽  
Maike Otto ◽  
...  
Keyword(s):  
Acetic Acid ◽  
Stationary Phase ◽  
Gene Knockout ◽  
Glucose Dehydrogenase ◽  
Gluconobacter Oxydans ◽  
Acetic Acid Bacteria ◽  
Acetic Acid Bacterium ◽  
Basal Expression ◽  
Fold Induction ◽  
Membrane Bound

Abstract The acetic acid bacterium (AAB) Gluconobacter oxydans incompletely oxidizes a wide variety of carbohydrates and is therefore used industrially for oxidative biotransformations. For G. oxydans, no system was available that allows regulatable plasmid-based expression. We found that the l-arabinose-inducible PBAD promoter and the transcriptional regulator AraC from Escherichia coli MC4100 performed very well in G. oxydans. The respective pBBR1-based plasmids showed very low basal expression of the reporters β-glucuronidase and mNeonGreen, up to 480-fold induction with 1% l-arabinose, and tunability from 0.1 to 1% l-arabinose. In G. oxydans 621H, l-arabinose was oxidized by the membrane-bound glucose dehydrogenase, which is absent in the multi-deletion strain BP.6. Nevertheless, AraC-PBAD performed similar in both strains in the exponential phase, indicating that a gene knockout is not required for application of AraC-PBAD in wild-type G. oxydans strains. However, the oxidation product arabinonic acid strongly contributed to the acidification of the growth medium in 621H cultures during the stationary phase, which resulted in drastically decreased reporter activities in 621H (pH 3.3) but not in BP.6 cultures (pH 4.4). These activities could be strongly increased quickly solely by incubating stationary cells in d-mannitol-free medium adjusted to pH 6, indicating that the reporters were hardly degraded yet rather became inactive. In a pH-controlled bioreactor, these reporter activities remained high in the stationary phase (pH 6). Finally, we created a multiple cloning vector with araC-PBAD based on pBBR1MCS-5. Together, we demonstrated superior functionality and good tunability of an AraC-PBAD system in G. oxydans that could possibly also be used in other AAB. Key points • We found the AraC-PBADsystem from E. coli MC4100 was well tunable in G. oxydans. •  In the absence of AraC orl-arabinose, expression from PBADwas extremely low. • This araC-PBADsystem could also be fully functional in other acetic acid bacteria.

scholarly journals Characterization and inactivation of the membrane-bound polyol dehydrogenase in Gluconobacter oxydans DSM 7145 reveals a role in meso-erythritol oxidation

Microbiology ◽  
2010 ◽  
Vol 156 (6) ◽  
pp. 1890-1899 ◽  
Author(s):  
Jörn Voss ◽  
Armin Ehrenreich ◽  
Wolfgang Liebl
Keyword(s):  
Acetic Acid ◽  
Gluconobacter Oxydans ◽  
Acetic Acid Bacteria ◽  
Second Phase ◽  
Growth Substrate ◽  
Whole Cell ◽  
Polyol Dehydrogenase ◽  
Membrane Bound ◽  
Two Stages ◽  
Substrate Spectrum

The growth of Gluconobacter oxydans DSM 7145 on meso-erythritol is characterized by two stages: in the first stage, meso-erythritol is oxidized almost stoichiometrically to l-erythrulose according to the Bertrand–Hudson rule. The second phase is distinguished from the first phase by a global metabolic change from membrane-bound meso-erythritol oxidation to l-erythrulose assimilation with concomitant accumulation of acetic acid. The membrane-associated erythritol-oxidizing enzyme was found to be encoded by a gene homologous to sldA known from other species of acetic acid bacteria. Disruption of this gene in the genome of G. oxydans DSM 7145 revealed that the membrane-bound polyol dehydrogenase not only oxidizes meso-erythritol but also has a broader substrate spectrum which includes C3–C6 polyols and d-gluconate and supports growth on these substrates. Cultivation of G. oxydans DSM 7145 on different substrates indicated that expression of the polyol dehydrogenase was not regulated, implying that the production of biomass of G. oxydans to be used as whole-cell biocatalysts in the biotechnological conversion of meso-erythritol to l-erythrulose, which is used as a tanning agent in the cosmetics industry, can be conveniently carried out with glucose as the growth substrate.

scholarly journals The inactive and active forms of the pyrroloquinoline quinone-alcohol dehydrogenase of Gluconacetobacter diazotrophicus: a comparative study

2013 ◽  
Vol 2 (1s) ◽  
pp. 2 ◽  
Author(s):  
Saul Gomez-Manzo ◽  
Irene Patricia Del Arenal-Mena ◽  
Edgardo Escamilla
Keyword(s):  
Acetic Acid ◽  
Alcohol Dehydrogenase ◽  
Comparative Study ◽  
Redox State ◽  
Catalytic Properties ◽  
Acetic Acid Bacteria ◽  
Pyrroloquinoline Quinone ◽  
Gluconacetobacter Diazotrophicus ◽  
Membrane Bound ◽  
Prosthetic Groups

<em>Gluconacetobacter diazotrophicus</em> as a member of the acetic acid bacteria group, oxidize alcohol to acetic acid through two sequential reactions catalyzed by the alcohol dehydrogenase (ADH) and the aldehyde dehydrogenase, both enzymes are membrane-bound and oriented to the periplasmic space. ADH is a quinohemoprotein carrying one pyrroloquinoline quinone moiety, one [2Fe:2S] cluster and four c-type cytochromes, as prosthetic groups. In recent years has been described the presence of the inactive ADH (ADHi) in the acetic acid bacteria. In the present review we make a comparative study of the molecular and catalytic properties of the active and inactive forms of ADH purified from <em>G. diazotrophicus</em>, variation in the redox state of enzymes <em>as purified </em>could explain the notorious differences seen in the activity power of the compared enzymes.

scholarly journals Crystallization of Membrane-bound Alcohol Dehydrogenase of Acetic Acid Bacteria

1982 ◽  
Vol 46 (11) ◽  
pp. 2859-2863
Author(s):  
Osao Adachi ◽  
Emiko Shinagawa ◽  
Kazunobu Matsushita ◽  
Minoru Ameyama
Keyword(s):  
Acetic Acid ◽  
Alcohol Dehydrogenase ◽  
Acetic Acid Bacteria ◽  
Membrane Bound

scholarly journals Pentose Oxidation by Acetic Acid Bacteria Led to a Finding of Membrane-Bound Purine Nucleosidase

2013 ◽  
Vol 77 (5) ◽  
pp. 1131-1133 ◽  
Author(s):  
Osao ADACHI ◽  
Roque A. HOURS ◽  
Yoshihiko AKAKABE ◽  
Emiko SHINAGAWA ◽  
Yoshitaka ANO ◽  
...  
Keyword(s):  
Acetic Acid ◽  
Acetic Acid Bacteria ◽  
Membrane Bound
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