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1

Spitaels, Freek, Anneleen Wieme, Tom Balzarini, Ilse Cleenwerck, Anita Van Landschoot, Luc De Vuyst, and Peter Vandamme. "Gluconobacter cerevisiae sp. nov., isolated from the brewery environment." International Journal of Systematic and Evolutionary Microbiology 64, Pt_4 (April 1, 2014): 1134–41. http://dx.doi.org/10.1099/ijs.0.059311-0.

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Three strains, LMG 27748T, LMG 27749 and LMG 27882 with identical MALDI-TOF mass spectra were isolated from samples taken from the brewery environment. Analysis of the 16S rRNA gene sequence of strain LMG 27748T revealed that the taxon it represents was closely related to type strains of the species Gluconobacter albidus (100 % sequence similarity), Gluconobacter kondonii (99.9 %), Gluconobacter sphaericus (99.9 %) and Gluconobacter kanchanaburiensis (99.5 %). DNA–DNA hybridization experiments on the type strains of these species revealed moderate DNA relatedness values (39–65 %). The three strains used d-fructose, d-sorbitol, meso-erythritol, glycerol, l-sorbose, ethanol (weakly), sucrose and raffinose as a sole carbon source for growth (weak growth on the latter two carbon sources was obtained for strains LMG 27748T and LMG 27882). The strains were unable to grow on glucose-yeast extract medium at 37 °C. They produced acid from meso-erythritol and sucrose, but not from raffinose. d-Gluconic acid, 2-keto-d-gluconic acid and 5-keto-d-gluconic acid were produced from d-glucose, but not 2,5-diketo-d-gluconic acid. These genotypic and phenotypic characteristics distinguish strains LMG 27748T, LMG 27749 and LMG 27882 from species of the genus Gluconobacter with validly published names and, therefore, we propose classifying them formally as representatives of a novel species, Gluconobacter cerevisiae sp. nov., with LMG 27748T ( = DSM 27644T) as the type strain.
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2

Jakob, Frank, Daniel Meißner, and Rudi F. Vogel. "Comparison of novel GH 68 levansucrases of levan-overproducing Gluconobacter species." Acetic Acid Bacteria 1, no. 1 (June 19, 2012): 2. http://dx.doi.org/10.4081/aab.2012.e2.

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<em>Gluconobacter</em> species are capable of incomplete oxidations which are exploited in food biotechnology. Levans isolated from exopolysaccharide (EPS)-overproducing <em>Gluconobacter</em> species are promising functional compounds for food applications. Fructan production strongly depends on the corresponding fructosyltransferases (Ftfs), which catalyze the formation of these polymers from sucrose. Therefore, we characterized novel Ftfs from three EPS-overproducing food-grade strains, i.e. <em>Gluconobacter</em> sp. TMW 2.767 and <em>Gluconobacter</em> sp. TMW 2.1191 isolated from water kefir, and <em>Gluconobacter cerinus</em> DSM 9533T isolated from cherries. Several PCR techniques, including degenerate gradient temperature PCR, modified and standard inverse PCR, modified site-finding PCR and modified single primer PCR, were used to finally detect complete open reading frames coding for Ftfs. The prospective ftf-gene sequences were heterologously expressed in <em>Escherichia coli</em> Top 10. <em>E. coli</em> transformants harboring one of the three different ftf-genes produced polysaccharides from sucrose in contrast to the <em>E. coli</em> wildtype. Each of the heterologously expressed proteins encoded a levansucrase, catalyzing the formation of b-(2&rarr;6)-linked fructose polymers, which corresponded to our previous analyses about the chemical nature of the isolated polymers formed by these <em>Gluconobacter</em> strains. Structurally, these enzymes belong to the glycoside hydrolase 68 family (GH 68), sharing the typical modular topology of levansucrases from gram-negative bacteria. In conclusion, we could identify novel active levansucrases, which can be used for <em>ex situ</em> (enzymatic catalyses) or <em>in situ</em> (fermentation) production of functional fructan polymers by <em>Gluconobacter</em> strains in food and other applications.
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3

Yukphan, Pattaraporn, Piyanat Charoenyingcharoen, Sukunphat Malimas, Yuki Muramatsu, Yasuyoshi Nakagawa, Somboon Tanasupawat, and Yuzo Yamada. "Gluconobacter aidae sp. nov., an acetic acid bacteria isolated from tropical fruits in Thailand." International Journal of Systematic and Evolutionary Microbiology 70, no. 7 (July 1, 2020): 4351–57. http://dx.doi.org/10.1099/ijsem.0.004292.

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Two bacterial strains, isolates AC10T and AC20, which were reported in a previous study on the diversity of acetic acid bacteria in Thailand, were subjected to a taxonomic study. The phylogenetic analysis based on the 16S rRNA gene sequences showed that the two isolates were located closely to the type strains of Gluconobacter oxydans and Gluconobacter roseus . However, the two isolates formed a separate cluster from the type strains of the two species. The genomic DNA of isolate AC10T was sequenced. The assembled genomes of the isolate were analysed for average nucleotide identity (ANI) and digital DNA–DNA hybridization (dDDH). The results showed that the highest ANI and dDDH values between isolate AC10T and G. oxydans DSM 3503T were 91.15 and 68.2 %, which are lower than the suggested values for species delineation. The genome-based tree was reconstructed and the phylogenetic lineage based on genome sequences showed that the lineage of isolate AC10T was distinct from G. oxydans DSM 3503T and its related species. The two isolates were distinguished from G. oxydans and their relatives by their phenotypic characteristics and MALDI-TOF profiles. Therefore, the two isolates, AC10T (=BCC 15749T=TBRC 11329T=NBRC 103576T) and AC20 (=BCC 15759=TBRC 11330=NBRC 103579), can be assigned to an independent species within the genus Gluconobacter , and the name Gluconobacter aidae sp. nov. is proposed for the two isolates.
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4

Keliang, Gao, and Wei Dongzhi. "Asymmetric oxidation by Gluconobacter oxydans." Applied Microbiology and Biotechnology 70, no. 2 (March 2006): 135–39. http://dx.doi.org/10.1007/s00253-005-0307-0.

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5

Vu, Huong Thi Lan, Oanh Thi Kim Nguyen, Van Thi Thu Bui, Uyen Thi Tu Bui, Nghiep Dai Ngo, Thao Thi Phuong Dang, and Pattaraporn Yukphan. "Isolation of dihydroxyacetone-producing acetic acid bacteria in Vietnam." Science and Technology Development Journal 19, no. 4 (December 31, 2016): 31–38. http://dx.doi.org/10.32508/stdj.v19i4.625.

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Sixty-six acetic acid bacteria (AAB) were isolated from fourty-five flowers and fruits collected in Hochiminh City, Vietnam. Of the sixty-six, thirty-one isolates were selected as dihydroxyacetone (DHA)-producing AAB based on the reaction with Fehling’s solution and grouped into three groups by routine identification with phenotypic features. Group I composed of fourteen isolates and was assigned to the genus Acetobacter, Group II composed of thirteen isolates and was assigned to the genus Gluconobacter and Group III was the remaining four isolates and was assigned to the genus Gluconacetobacter. Ten isolates among the thirteen isolates of Group II gave a larger amount of DHA (22.2–26.0 mg/mL) than Gluconobacter oxydans NBRC 14819T (19.8 mg/mL), promising for the potential use in producing DHA. In phylogenetic analysis based on 16S rRNA gene sequences, six isolates of the ten potential DHA producers were suggested to be candidates for new taxa in the genus Gluconobacter.
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6

Zhang, Jie Bing, Xiao Li Zhang, Duan Hao Wang, Bin Xia Zhao, and Gang He. "Biocatalytic Regioselective Oxidation of N-Hydroxyethyl Glucamine for Synthesis of Miglitol." Advanced Materials Research 197-198 (February 2011): 51–55. http://dx.doi.org/10.4028/www.scientific.net/amr.197-198.51.

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N-2-hydroxyethyl-glucamine (NHEG) was converted into 6-deoxy-6-hydroxylethyl-amino-L-sorbose (DHES) by the regioselective oxidation of Gluconobacter oxydans, and then the generated intermediate of this process was produced to N-hydroxyethyl-deoxynojirimycin (Miglitol) by reductive ring closure reaction. Regioselective oxidation reaction was catalyzed by the high activity sorbitol dehydrogenase of Gluconobacter oxydans biomass which was obtained in preliminary studies. Reductive ring closure reaction was carried out under the conditions of 10%Pd/C as catalyst, at 45~55°C and 0.6MPa of hydrogen. Reaction mixture by the separation and purification of strong acidic exchange resin column has been the Miglitol. In addition, the structure and properties of synthetic product was characterized by thin layer chromatography (TLC), melting point, mass spectrometry (MALDI-MS), Fourier transform infrared spectroscopy (FTIR) analysis. The results showed that the miglitol yield is 77.3%.The regional specificity of the high activity sorbitol dehydrogenase of Gluconobacter oxydans has been verified. Moreover, combinating the technology of the Pd/C- catalyzed reductive ring closure reaction, an effective synthesis process of miglitol is achieved.
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7

Schiessl, Jacqueline, Konrad Kosciow, Laura S. Garschagen, Juliane J. Hoffmann, Julia Heymuth, Thomas Franke, and Uwe Deppenmeier. "Degradation of the low-calorie sugar substitute 5-ketofructose by different bacteria." Applied Microbiology and Biotechnology 105, no. 6 (February 22, 2021): 2441–53. http://dx.doi.org/10.1007/s00253-021-11168-3.

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Abstract There is an increasing public awareness about the danger of dietary sugars with respect to their caloric contribution to the diet and the rise of overweight throughout the world. Therefore, low-calorie sugar substitutes are of high interest to replace sugar in foods and beverages. A promising alternative to natural sugars and artificial sweeteners is the fructose derivative 5-keto-D-fructose (5-KF), which is produced by several Gluconobacter species. A prerequisite before 5-KF can be used as a sweetener is to test whether the compound is degradable by microorganisms and whether it is metabolized by the human microbiota. We identified different environmental bacteria (Tatumella morbirosei, Gluconobacter japonicus LMG 26773, Gluconobacter japonicus LMG 1281, and Clostridium pasteurianum) that were able to grow with 5-KF as a substrate. Furthermore, Gluconobacter oxydans 621H could use 5-KF as a carbon and energy source in the stationary growth phase. The enzymes involved in the utilization of 5-KF were heterologously overproduced in Escherichia coli, purified and characterized. The enzymes were referred to as 5-KF reductases and belong to three unrelated enzymatic classes with highly different amino acid sequences, activities, and structural properties. Furthermore, we could show that 15 members of the most common and abundant intestinal bacteria cannot degrade 5-KF, indicating that this sugar derivative is not a suitable growth substrate for prokaryotes in the human intestine. Key points • Some environmental bacteria are able to use 5-KF as an energy and carbon source. • Four 5-KF reductases were identified, belonging to three different protein families. • Many gut bacteria cannot degrade 5-KF.
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8

Kommanee, Jintana, Somboon Tanasupawat, Pattaraporn Yukphan, Taweesak Malimas, Yuki Muramatsu, Yasuyoshi Nakagawa, and Yuzo Yamada. "Gluconobacter nephelii sp. nov., an acetic acid bacterium in the class Alphaproteobacteria." International Journal of Systematic and Evolutionary Microbiology 61, no. 9 (September 1, 2011): 2117–22. http://dx.doi.org/10.1099/ijs.0.026385-0.

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Three strains, RBY-1T, PHD-1 and PHD-2, were isolated from fruits in Thailand. The strains were Gram-negative, aerobic rods with polar flagella, produced acetic acid from ethanol and did not oxidize acetate or lactate. In phylogenetic trees based on 16S rRNA gene sequences and 16S–23S rRNA gene internal transcribed spacer (ITS) sequences, the strains formed a cluster separate from the type strains of recognized species of the genus Gluconobacter. The calculated 16S rRNA gene sequence and 16S–23S rRNA gene ITS sequence similarities were respectively 97.7–99.7 % and 77.3–98.1 %. DNA G+C contents ranged from 57.2 to 57.6 mol%. The strains showed high DNA–DNA relatedness of 100 % to one another, but low DNA–DNA relatedness of 11–34 % to the tested type strains of recognized Gluconobacter species. Q-10 was the major quinone. On the basis of the genotypic and phenotypic data obtained, the three strains clearly represent a novel species, for which the name Gluconobacter nephelii sp. nov. is proposed. The type strain is RBY-1T ( = BCC 36733T = NBRC 106061T = PCU 318T), whose DNA G+C content is 57.2 mol%.
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9

Sethi, Madhuresh K., Anish Kumar, Nagaraj Maddur, Rohit Shukla, and Lakshmi Narayana Vemula. "Gluconobacter mediated synthesis of amino sugars." Journal of Molecular Catalysis B: Enzymatic 112 (February 2015): 54–58. http://dx.doi.org/10.1016/j.molcatb.2014.12.003.

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10

Ricelli, A., F. Baruzzi, M. Solfrizzo, M. Morea, and F. P. Fanizzi. "Biotransformation of Patulin by Gluconobacter oxydans." Applied and Environmental Microbiology 73, no. 3 (November 17, 2006): 785–92. http://dx.doi.org/10.1128/aem.02032-06.

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ABSTRACT A bacterium isolated from patulin-contaminated apples was capable of degrading patulin to a less-toxic compound, ascladiol. The bacterium was identified as Gluconobacter oxydans by 16S rRNA gene sequencing, whereas ascladiol was identified by liquid chromatography-tandem mass spectrometry and proton and carbon nuclear magnetic resonance. Degradation of up to 96% of patulin was observed in apple juices containing up to 800 μg/ml of patulin and incubated with G. oxydans.
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11

Qazi, G. N., R. Parshad, V. Verma, C. L. Chopra, R. Buse, M. Träger, and U. Onken. "Diketo-gluconate fermentation by Gluconobacter oxydans." Enzyme and Microbial Technology 13, no. 6 (June 1991): 504–7. http://dx.doi.org/10.1016/0141-0229(91)90010-8.

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12

Lee, Young Sun, Jae Young Kim, Mi Yeon Cha, and Hee Cheol Kang. "Characteristics of Biocellulose by Gluconobacter uchimurae GYS15." Journal of the Society of Cosmetic Scientists of Korea 42, no. 3 (September 30, 2016): 247–55. http://dx.doi.org/10.15230/scsk.2016.42.3.247.

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13

Creaven, Martina, Richard J. Fitzgerald, and Fergal O'Gara. "Transformation of Gluconobacter oxydans subsp. suboxydans by electroporation." Canadian Journal of Microbiology 40, no. 6 (June 1, 1994): 491–94. http://dx.doi.org/10.1139/m94-079.

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An efficient electroporation system for Gluconobacter oxydans subsp. suboxydans was developed that gave transformation frequencies of up to 105 transformants/μg of DNA. The system was studied with respect to different operating parameters including (i) the effect of electrical conditions, i.e., field strength and resistance, (ii) DNA concentration, (iii) composition of the electroporation buffer, (iv) initial cell concentration, and (v) stage of growth of the cells. Optimal electroporation conditions were found under the following conditions: 12.5 kV/cm field strength, 400 ? parallel resistor setting, 0.4–0.5 μg DNA/100 μL cell suspension, and electroporation buffer containing Mg ions and > 1011 colony-forming units/mL of early to mid log phase cells.Key words: Gluconobacter suboxydans, electroporation, field strength.
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14

Roh, Seong Woon, Young-Do Nam, Ho-Won Chang, Kyoung-Ho Kim, Min-Soo Kim, Ji-Hwan Ryu, Sung-Hee Kim, Won-Jae Lee, and Jin-Woo Bae. "Phylogenetic Characterization of Two Novel Commensal Bacteria Involved with Innate Immune Homeostasis in Drosophila melanogaster." Applied and Environmental Microbiology 74, no. 20 (August 22, 2008): 6171–77. http://dx.doi.org/10.1128/aem.00301-08.

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ABSTRACT During a previous study on the molecular interaction between commensal bacteria and host gut immunity, two novel bacterial strains, A911T and G707T, were isolated from the gut of Drosophila melanogaster. In this study, these strains were characterized in a polyphasic taxonomic study using phenotypic, genetic, and chemotaxonomic analyses. We show that the strains represent novel species in the family Acetobacteraceae. Strain G707T, a highly pathogenic organism, represents a new species in the genus Gluconobacter, “Gluconobacter morbifer” sp. nov. (type strain G707 = KCTC 22116T = JCM 15512T). Strain A911T, dominantly present in the normal Drosphila gut community, represents a novel genus and species, designated “Commensalibacter intestini” gen. nov., sp. nov. (type strain A911 = KCTC 22117T = JCM 15511T).
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15

Tang, Wen, Lulu Chen, Jian Deng, Yuyao Kuang, Chao Chen, Bo Yin, Hualei Wang, Jinping Lin, and Dongzhi Wei. "Structure-guided evolution of carbonyl reductase for efficient biosynthesis of ethyl (R)-2-hydroxy-4-phenylbutyrate." Catalysis Science & Technology 10, no. 22 (2020): 7512–22. http://dx.doi.org/10.1039/d0cy01411g.

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16

Švitel, Juraj, Jan Tkáč, Igor Voštiar, Marian Navrátil, Vladimír Štefuca, Marek Bučko, and Peter Gemeiner. "Gluconobacter in biosensors: applications of whole cells and enzymes isolated from gluconobacter and acetobacter to biosensor construction." Biotechnology Letters 28, no. 24 (October 28, 2006): 2003–10. http://dx.doi.org/10.1007/s10529-006-9195-3.

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17

Švitel, Juraj, Jan Tkáč, Igor Voštiar, Marian Navrátil, Vladimír Štefuca, Marek Bučko, and Peter Gemeiner. "Gluconobacter in biosensors: applications of whole cells and enzymes isolated from Gluconobacter and Acetobacter to biosensor construction." Biotechnology Letters 29, no. 3 (February 6, 2007): 509. http://dx.doi.org/10.1007/s10529-006-9307-0.

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18

Kuska, Justyna, Freya Taday, Kathryn Yeow, James Ryan, and Elaine O'Reilly. "An in vitro–in vivo sequential cascade for the synthesis of iminosugars from aldoses." Catalysis Science & Technology 11, no. 13 (2021): 4327–31. http://dx.doi.org/10.1039/d1cy00698c.

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Here, we report a chemoenzymatic approach for the preparation of a small panel of biologically important iminosugars from readily available aldoses, employing a transaminase in combination with Gluconobacter oxydans whole cells.
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19

Watanabe, Hikaru, Chong Han Ng, Vachiranee Limviphuvadh, Shinya Suzuki, and Takuji Yamada. "Gluconobacter dominates the gut microbiome of the Asian palm civet Paradoxurus hermaphroditus that produces kopi luwak." PeerJ 8 (July 30, 2020): e9579. http://dx.doi.org/10.7717/peerj.9579.

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Coffee beans derived from feces of the civet cat are used to brew coffee known as kopi luwak (the Indonesian words for coffee and palm civet, respectively), which is one of the most expensive coffees in the world owing to its limited supply and strong market demand. Recent metabolomics studies have revealed that kopi luwak metabolites differ from metabolites found in other coffee beans. To produce kopi luwak, coffee beans are first eaten by civet cats. It has been proposed that fermentation inside the civet cat digestive tract may contribute to the distinctively smooth flavor of kopi luwak, but the biological basis has not been determined. Therefore, we characterized the microbiome of civet cat feces using 16S rRNA gene sequences to determine the bacterial taxa that may influence fermentation processes related to kopi luwak. Moreover, we compared this fecal microbiome with that of 14 other animals, revealing that Gluconobacter is a genus that is, uniquely found in feces of the civet cat. We also found that Gluconobacter species have a large number of cell motility genes, which may encode flagellar proteins allowing colonization of the civet gut. In addition, genes encoding enzymes involved in the metabolism of hydrogen sulfide and sulfur-containing amino acids were over-represented in Gluconobacter. These genes may contribute to the fermentation of coffee beans in the digestive tract of civet cats.
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20

Ohrem, H. Leonhard, and Harald Voβ. "Kinetics of polyol oxidation with Gluconobacter oxydans." Biotechnology Letters 17, no. 11 (November 1995): 1195–200. http://dx.doi.org/10.1007/bf00128385.

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21

Ohrem, H. Leonhard, and Harald Voβ. "Inhibitory effects of dihydroxyacetone on Gluconobacter cultures." Biotechnology Letters 17, no. 9 (September 1995): 981–84. http://dx.doi.org/10.1007/bf00127438.

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22

Naessens, Myriam, An Cerdobbel, Wim Soetaert, and Erick J. Vandamme. "Dextran dextrinase and dextran of Gluconobacter oxydans." Journal of Industrial Microbiology & Biotechnology 32, no. 8 (June 23, 2005): 323–34. http://dx.doi.org/10.1007/s10295-005-0259-5.

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23

U., Deppenmeier, Hoffmeister M., and Prust C. "Biochemistry and biotechnological applications of Gluconobacter strains." Applied Microbiology and Biotechnology 60, no. 3 (November 1, 2002): 233–42. http://dx.doi.org/10.1007/s00253-002-1114-5.

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Buchert, Johanna, and Liisa Viikari. "Oxidative d-xylose metabolism of Gluconobacter oxydans." Applied Microbiology and Biotechnology 29, no. 4 (October 1988): 375–79. http://dx.doi.org/10.1007/bf00265822.

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Ohrem, H. Leonhard, and Harald Voβ. "Inhibitory effects of glycerol on Gluconobacter oxydans." Biotechnology Letters 18, no. 3 (March 1996): 245–50. http://dx.doi.org/10.1007/bf00142939.

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26

Katsura, K. "Gluconobacter asaii Mason and Claus 1989 is a junior subjective synonym of Gluconobacter cerinus Yamada and Akita 1984." INTERNATIONAL JOURNAL OF SYSTEMATIC AND EVOLUTIONARY MICROBIOLOGY 52, no. 5 (September 1, 2002): 1635–40. http://dx.doi.org/10.1099/ijs.0.02093-0.

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27

Katsura, Kazushige, Yuzo Yamada, Tai Uchimura, and Kazuo Komagata. "Gluconobacter asaii Mason and Claus 1989 is a junior subjective synonym of Gluconobacter cerinus Yamada and Akita 1984." International Journal of Systematic and Evolutionary Microbiology 52, no. 5 (September 1, 2002): 1635–40. http://dx.doi.org/10.1099/00207713-52-5-1635.

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28

Matsushita, Kazunobu, Yoshikazu Fujii, Yoshitaka Ano, Hirohide Toyama, Masako Shinjoh, Noribumi Tomiyama, Taro Miyazaki, Teruhide Sugisawa, Tatsuo Hoshino, and Osao Adachi. "5-Keto-d-Gluconate Production Is Catalyzed by a Quinoprotein Glycerol Dehydrogenase, Major Polyol Dehydrogenase, in Gluconobacter Species." Applied and Environmental Microbiology 69, no. 4 (April 2003): 1959–66. http://dx.doi.org/10.1128/aem.69.4.1959-1966.2003.

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ABSTRACT Acetic acid bacteria, especially Gluconobacter species, have been known to catalyze the extensive oxidation of sugar alcohols (polyols) such as d-mannitol, glycerol, d-sorbitol, and so on. Gluconobacter species also oxidize sugars and sugar acids and uniquely accumulate two different keto-d-gluconates, 2-keto-d-gluconate and 5-keto-d-gluconate, in the culture medium by the oxidation of d-gluconate. However, there are still many controversies regarding their enzyme systems, especially on d-sorbitol and also d-gluconate oxidations. Recently, pyrroloquinoline quinone-dependent quinoprotein d-arabitol dehydrogenase and d-sorbitol dehydrogenase have been purified from G. suboxydans, both of which have similar and broad substrate specificity towards several different polyols. In this study, both quinoproteins were shown to be identical based on their immuno-cross-reactivity and also on gene disruption and were suggested to be the same as the previously isolated glycerol dehydrogenase (EC 1.1.99.22). Thus, glycerol dehydrogenase is the major polyol dehydrogenase involved in the oxidation of almost all sugar alcohols in Gluconobacter sp. In addition, the so-called quinoprotein glycerol dehydrogenase was also uniquely shown to oxidize d-gluconate, which was completely different from flavoprotein d-gluconate dehydrogenase (EC 1.1.99.3), which is involved in the production of 2-keto-d-gluconate. The gene disruption experiment and the reconstitution system of the purified enzyme in this study clearly showed that the production of 5-keto-d-gluconate in G. suboxydans is solely dependent on the quinoprotein glycerol dehydrogenase.
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Adelgareeva, A. Yu, S. N. Starikov, E. E. Stupak, and T. V. Markusheva. "SCREENING OF ENCODING CHLORAMPHENICOL RESISTANCE catA1 GENE IN THE BACTERIA OF TECHNOGENIC ECOTOPES." ÈKOBIOTEH 3, no. 4 (2020): 722–26. http://dx.doi.org/10.31163/2618-964x-2020-3-4-722-726.

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The catA1 gene was screened in microorganisms of the Republic of Bashkortostan industrial ecotopes. Encoding antibiotic chloramphenicol enzymic inactivation catA1 - like sequences were not found in the bacteria of the Aeromonas, Agromyces, Bacillus, Citrobacter, Gluconobacter, Rhodococcus and Serratia genera.
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Saichana, Ittipon, Duangtip Moonmangmee, Osao Adachi, Kazunobu Matsushita, and Hirohide Toyama. "Screening of Thermotolerant Gluconobacter Strains for Production of 5-Keto-d-Gluconic Acid and Disruption of Flavin Adenine Dinucleotide-Containing d-Gluconate Dehydrogenase." Applied and Environmental Microbiology 75, no. 13 (May 1, 2009): 4240–47. http://dx.doi.org/10.1128/aem.00640-09.

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ABSTRACT We isolated thermotolerant Gluconobacter strains that are able to produce 5-keto-d-gluconic acid (5KGA) at 37°C, a temperature at which regular mesophilic 5KGA-producing strains showed much less growth and 5KGA production. The thermotolerant strains produced 2KGA as the major product at both 30 and 37°C. The amount of ketogluconates produced at 37°C was slightly less than the amount produced at 30°C. To improve the yield of 5KGA in these strains, we disrupted flavin adenine dinucleotide-gluconate dehydrogenase (FAD-GADH), which is responsible for 2KGA production. Genes for FAD-GADH were cloned by using inverse PCR and an in vitro cloning strategy. The sequences obtained for three thermotolerant strains were identical and showed high levels of identity to the FAD-GADH sequence reported for the genome of Gluconobacter oxydans 621 H. A kanamycin resistance gene cassette was used to disrupt the FAD-GADH genes in the thermotolerant strains. The mutant strains produced 5KGA exclusively, and the final yields were over 90% at 30°C and 50% at 37°C. We found that the activity of pyrroloquinoline quinone (PQQ)-dependent glycerol dehydrogenase, which is responsible for 5KGA production, increased in response to addition of PQQ and CaCl2 in vitro when cells were grown at 37°C. Addition of 5 mM CaCl2 to the culture medium of the mutant strains increased 5KGA production to the point where over 90% of the initial substrate was converted. The thermotolerant Gluconobacter strains that we isolated in this study provide a promising new option for industrial 5KGA production.
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Matsutani, Minenosuke, Haruo Suzuki, Toshiharu Yakushi, and Kazunobu Matsushita. "Draft genome sequence of Gluconobacter thailandicus NBRC 3257." Standards in Genomic Sciences 9, no. 3 (February 1, 2014): 614–23. http://dx.doi.org/10.4056/sigs.4778605.

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Felder, M. "The pyrroloquinoline quinone synthesis genes of Gluconobacter oxydans." FEMS Microbiology Letters 193, no. 2 (December 15, 2000): 231–36. http://dx.doi.org/10.1016/s0378-1097(00)00487-0.

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Valach, Milan, Jaroslav Katrlík, Ernest Šturdík, and Peter Gemeiner. "Ethanol Gluconobacter biosensor designed for flow injection analysis." Sensors and Actuators B: Chemical 138, no. 2 (May 2009): 581–86. http://dx.doi.org/10.1016/j.snb.2009.02.017.

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Schweikert, S., T. Polen, S. Bringer-Meyer, and M. Bott. "Physiologie und Regulation des Zuckerkatabolismus in Gluconobacter oxydans." Chemie Ingenieur Technik 82, no. 9 (August 27, 2010): 1556. http://dx.doi.org/10.1002/cite.201050453.

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Schweiger, Paul, and Uwe Deppenmeier. "Analysis of aldehyde reductases from Gluconobacter oxydans 621H." Applied Microbiology and Biotechnology 85, no. 4 (July 31, 2009): 1025–31. http://dx.doi.org/10.1007/s00253-009-2154-x.

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Molinari, F., R. Villa, M. Manzoni, and F. Aragozzini. "Aldehyde production by alcohol oxidation with Gluconobacter oxydans." Applied Microbiology and Biotechnology 43, no. 6 (November 1995): 989–94. http://dx.doi.org/10.1007/bf00166914.

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Albin, Andreas, Johannes Bader, Edeltraud Mast-Gerlach, and Ulf Stahl. "Improving fermentation and biomass formation of Gluconobacter oxydans." Journal of Biotechnology 131, no. 2 (September 2007): S160—S161. http://dx.doi.org/10.1016/j.jbiotec.2007.07.884.

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Qazi, G. N., V. Verma, R. Parshad, and C. L. Chopra. "Plasmid-mediated direct-glucose oxidation in Gluconobacter oxydans." Journal of Biotechnology 10, no. 1 (April 1989): 85–88. http://dx.doi.org/10.1016/0168-1656(89)90094-1.

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Liu, Li, Yue Chen, Shiqin Yu, Jian Chen, and Jingwen Zhou. "Simultaneous transformation of five vectors in Gluconobacter oxydans." Plasmid 117 (September 2021): 102588. http://dx.doi.org/10.1016/j.plasmid.2021.102588.

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Kaushal, Naveet. "Vinegar Production from Barley Malt using Immobilized Gluconobacter oxydans." International Journal of Pure & Applied Bioscience 5, no. 5 (November 30, 2017): 264–71. http://dx.doi.org/10.18782/2320-7051.5773.

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Islami, M., A. Shabani, M. Saifi-Abol, Sh Sepehr, M. R. Soudi, and S. Z. Mossavi-Ne. "Purification and Characterization of Alcohol Dehydrogenase from Gluconobacter suboxydans." Pakistan Journal of Biological Sciences 11, no. 2 (January 1, 2008): 208–13. http://dx.doi.org/10.3923/pjbs.2008.208.213.

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Sims, I. M., A. Thomson, U. Hubl, N. G. Larsen, and R. H. Furneaux. "Characterisation of polysaccharides synthesised by Gluconobacter oxydans NCIMB 4943." Carbohydrate Polymers 45, no. 3 (July 2001): 285–92. http://dx.doi.org/10.1016/s0144-8617(00)00262-9.

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ROBAKIS, N. K., N. J. PALLERONI, C. W. DESPREAUX, M. BOUBLIK, C. A. BAKER, P. J. CHURN, and G. W. CLAUS. "Isolation and Characterization of two Phages for Gluconobacter oxydans." Microbiology 131, no. 9 (September 1, 1985): 2467–73. http://dx.doi.org/10.1099/00221287-131-9-2467.

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FUKAYA, Masahiro, Hajime OKUMURA, Hiroshi MASAI, Takeshi UOZUMI, and Teruhiko BEPPU. "Development of a host-vector system for Gluconobacter suboxydans." Agricultural and Biological Chemistry 49, no. 8 (1985): 2407–11. http://dx.doi.org/10.1271/bbb1961.49.2407.

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Matsutani, Minenosuke, Hideki Hirakawa, Toshiharu Yakushi, and Kazunobu Matsushita. "Genome-wide phylogenetic analysis of Gluconobacter, Acetobacter, and Gluconacetobacter." FEMS Microbiology Letters 315, no. 2 (December 23, 2010): 122–28. http://dx.doi.org/10.1111/j.1574-6968.2010.02180.x.

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Micales, B. K., J. L. Johnson, and G. W. Claus. "Deoxyribonucleic Acid Homologies Among Organisms in the Genus Gluconobacter." International Journal of Systematic Bacteriology 35, no. 1 (January 1, 1985): 79–85. http://dx.doi.org/10.1099/00207713-35-1-79.

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Nanduri, V. B., A. Banerjee, J. M. Howell, D. B. Brzozowski, R. F. Eiring, and R. N. Patel. "Purification of a stereospecific 2-ketoreductase from Gluconobacter oxydans." Journal of Industrial Microbiology and Biotechnology 25, no. 3 (September 1, 2000): 171–75. http://dx.doi.org/10.1038/sj.jim.7000047.

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Kondo, K., and S. Horinouchi. "Characterization of an insertion sequence, IS12528, from Gluconobacter suboxydans." Applied and environmental microbiology 63, no. 3 (1997): 1139–42. http://dx.doi.org/10.1128/aem.63.3.1139-1142.1997.

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Claret, C., J. M. Salmon, C. Romieu, and A. Bories. "Physiology of Gluconobacter oxydans during dihydroxyacetone production from glycerol." Applied Microbiology and Biotechnology 41, no. 3 (May 1, 1994): 359–65. http://dx.doi.org/10.1007/s002530050157.

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Zahid, Nageena, Paul Schweiger, Erwin Galinski, and Uwe Deppenmeier. "Identification of mannitol as compatible solute in Gluconobacter oxydans." Applied Microbiology and Biotechnology 99, no. 13 (May 16, 2015): 5511–21. http://dx.doi.org/10.1007/s00253-015-6626-x.

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