Gluconobacter: A genus of gram-negative, rod-shaped to ellipsoidal bacteria occurring singly or in pairs and found in flowers, soil, honey bees, fruits, cider, beer, wine, and vinegar. (From Bergey's Manual of Determinative Bacteriology, 9th ed)Gluconobacter oxydans: A rod-shaped to ellipsoidal, gram-negative bacterium which oxidizes ethanol to acetic acid and prefers sugar-enriched environments. (From Bergey's Manual of Determinative Bacteriology, 9th ed)Pseudomonadaceae: A family of gram-negative bacteria usually found in soil or water and including many plant pathogens and a few animal pathogens.Acetobacteraceae: A family of gram-negative aerobic bacteria consisting of ellipsoidal to rod-shaped cells that occur singly, in pairs, or in chains.Sorbose: A ketose sugar that is commonly used in the commercial synthesis of ASCORBIC ACID.L-Iditol 2-Dehydrogenase: An alcohol oxidoreductase which catalyzes the oxidation of L-iditol to L-sorbose in the presence of NAD. It also acts on D-glucitol to form D-fructose. It also acts on other closely related sugar alcohols to form the corresponding sugar. EC 1.1.1.14Acetobacter: A species of gram-negative bacteria of the family ACETOBACTERACEAE found in FLOWERS and FRUIT. Cells are ellipsoidal to rod-shaped and straight or slightly curved.Sugar Alcohol Dehydrogenases: Reversibly catalyzes the oxidation of a hydroxyl group of sugar alcohols to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2. and EC 1.1.99.GluconatesCarbohydrate Dehydrogenases: Reversibly catalyze the oxidation of a hydroxyl group of carbohydrates to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2.; and 1.1.99.Sorbitol: A polyhydric alcohol with about half the sweetness of sucrose. Sorbitol occurs naturally and is also produced synthetically from glucose. It was formerly used as a diuretic and may still be used as a laxative and in irrigating solutions for some surgical procedures. It is also used in many manufacturing processes, as a pharmaceutical aid, and in several research applications.Dihydroxyacetone: A ketotriose compound. Its addition to blood preservation solutions results in better maintenance of 2,3-diphosphoglycerate levels during storage. It is readily phosphorylated to dihydroxyacetone phosphate by triokinase in erythrocytes. In combination with naphthoquinones it acts as a sunscreening agent.PQQ Cofactor: A pyrrolo-quinoline having two adjacent keto-groups at the 4 and 5 positions and three acidic carboxyl groups. It is a coenzyme of some DEHYDROGENASES.Sugar Alcohols: Polyhydric alcohols having no more than one hydroxy group attached to each carbon atom. They are formed by the reduction of the carbonyl group of a sugar to a hydroxyl group.(From Dorland, 28th ed)Xylulose: A 5-carbon keto sugar.Glucose 1-Dehydrogenase: A glucose dehydrogenase that catalyzes the oxidation of beta-D-glucose to form D-glucono-1,5-lactone, using NAD as well as NADP as a coenzyme.Acetic Acid: Product of the oxidation of ethanol and of the destructive distillation of wood. It is used locally, occasionally internally, as a counterirritant and also as a reagent. (Stedman, 26th ed)Xylitol: A five-carbon sugar alcohol derived from XYLOSE by reduction of the carbonyl group. It is as sweet as sucrose and used as a noncariogenic sweetener.Glyceric AcidsGlucose Dehydrogenases: D-Glucose:1-oxidoreductases. Catalyzes the oxidation of D-glucose to D-glucono-gamma-lactone and reduced acceptor. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.47; EC 1.1.1.118; EC 1.1.1.119 and EC 1.1.99.10.D-Xylulose Reductase: An enzyme that plays a role in the PENTOSES and GLUCURONATES interconversion pathway by catalyzing the oxidation of XYLITOL to D-xylulose. This enzyme has been found to be specific for NAD+.DNA, Ribosomal Spacer: The intergenic DNA segments that are between the ribosomal RNA genes (internal transcribed spacers) and between the tandemly repeated units of rDNA (external transcribed spacers and nontranscribed spacers).Ribitol: A sugar alcohol formed by the reduction of ribose.Shikimic Acid: A tri-hydroxy cyclohexene carboxylic acid important in biosynthesis of so many compounds that the shikimate pathway is named after it.Alphaproteobacteria: A class in the phylum PROTEOBACTERIA comprised mostly of two major phenotypes: purple non-sulfur bacteria and aerobic bacteriochlorophyll-containing bacteria.KetosesSugar AcidsMethylphenazonium Methosulfate: Used as an electron carrier in place of the flavine enzyme of Warburg in the hexosemonophosphate system and also in the preparation of SUCCINIC DEHYDROGENASE.Ubiquinone: A lipid-soluble benzoquinone which is involved in ELECTRON TRANSPORT in mitochondrial preparations. The compound occurs in the majority of aerobic organisms, from bacteria to higher plants and animals.RNA, Ribosomal, 16S: Constituent of 30S subunit prokaryotic ribosomes containing 1600 nucleotides and 21 proteins. 16S rRNA is involved in initiation of polypeptide synthesis.Alcohol Dehydrogenase: A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen.Alcohol Oxidoreductases: A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).RNA, Ribosomal, 23S: Constituent of 50S subunit of prokaryotic ribosomes containing about 3200 nucleotides. 23S rRNA is involved in the initiation of polypeptide synthesis.Glycerol: A trihydroxy sugar alcohol that is an intermediate in carbohydrate and lipid metabolism. It is used as a solvent, emollient, pharmaceutical agent, and sweetening agent.DNA, Bacterial: Deoxyribonucleic acid that makes up the genetic material of bacteria.Base Composition: The relative amounts of the PURINES and PYRIMIDINES in a nucleic acid.

*  KEGG PATHWAY: Citrate cycle (TCA cycle) - Gluconobacter oxydans H24

Citrate cycle (TCA cycle) - Gluconobacter oxydans H24 [ Pathway menu , Organism menu , Pathway entry , Download KGML , Show ...
genome.jp/kegg-bin/show_pathway?goh00020

*  UniProt: Q5FRH4 GLUOX

Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans). OC Bacteria; Proteobacteria; Alphaproteobacteria; ... Rhodospirillales; OC Acetobacteraceae; Gluconobacter. OX NCBI_TaxID=290633 {ECO:0000313,EMBL:AAW61022.1, ECO:0000313,Proteomes: ... "Complete genome sequence of the acetic acid bacterium Gluconobacter RT oxydans."; RL Nat. Biotechnol. 23:195-200(2005). CC ...
genome.jp/dbget-bin/www_bget?uniprot:Q5FRH4_GLUOX

*  DSM 2343 Strain Browser - StrainInfo

Gluconobacter oxydans. Direct link to DSM 2343 catalog. ...
straininfo.net/strains/12017/browser

*  cosmetic Ingredients Information Catalog : Starting with g

gluconobacter/honey ferment filtrate. Use(s): cosmetic ingredient for skin and hair conditioning. ...
thegoodscentscompany.com/cosng-g.htm

*  Alcohol deshidrogenasa (quinona) - Wikipedia

Gluconobacter suboxydans». Biosci. Biotechnol. Biochem. 72 (10): 2723-2731. PMID 18838797. doi:10.1271/bbb.80363. Matsushita, K ... electron transport and ubiquinone reduction in the quinohemoprotein alcohol dehydrogenase-cytochrome c complex of Gluconobacter ... with ubiquinone of pyrroloquinoline quinone-dependent alcohol dehydrogenases purified from Acetobacter aceti and Gluconobacter ...
https://es.wikipedia.org/wiki/Alcohol_deshidrogenasa_(quinona)

*  Microbiologist, September 2015 by Society for Applied Microbiology - issuu

Aeromonas Borrelia Microbacterium Rheinheimera Wautersiella Saccharopolyspora Rahnella Nocardioides Gluconobacter Xanthobacter ... Castellaniella Borrelia Microbacterium Rheinheimera Wautersiella Saccharopolyspora Rahnella Nocardioides Gluconobacter ...
https://issuu.com/societyforappliedmicrobiology/docs/microbiologistseptemberweb

*  BRENDA - Information on EC 1.1.1.264 - L-idonate 5-dehydrogenase

Gluconobacter cerinus, Gluconobacter gluconicus, Gluconobacter oxydans, Gluconobacter roseus, Gluconobacter sphaericus ... Crystallization and properties of 5-keto-D-gluconate reductase from Gluconobacter suboxydans ... Acetobacter aceti, Frateuria aurantia, Gluconacetobacter liquefaciens, Gluconobacter albidus, ...
brenda-enzymes.info/enzyme.php?ecno=1.1.1.264

*  pCOMP - Predicted Chlamydia Outer Membrane Proteins

Gluconobacter oxydans 621H. RND-type multidrug efflux pump, outer membrane protein. n.d.. ...
131.130.66.201/pcomp/browse.asp?clusterid=13

*  pCOMP - Predicted Chlamydia Outer Membrane Proteins

Gluconobacter oxydans 621H. Outer membrane channel protein. n.d.. GOX0689. Gluconobacter oxydans 621H. Probable outer membrane ...
131.130.66.201/pcomp/browse.asp?clusterid=15

*  pCOMP - Predicted Chlamydia Outer Membrane Proteins

Gluconobacter oxydans 621H. Outer membrane protein. n.d.. GbCGDNIH1_. Granulibacter bethesdensis CGDNIH1. outer membrane ...
131.130.66.201/pcomp/browse.asp?clusterid=19

*  pCOMP - Predicted Chlamydia Outer Membrane Proteins

Gluconobacter oxydans 621H. Peptidyl-prolyl cis-trans isomerase. n.d.. GFO_2538. Gramella forsetii KT0803. cyclophilin/FKBP- ...
131.130.66.201/pcomp/browse.asp?clusterid=14

*  pCOMP - Predicted Chlamydia Outer Membrane Proteins

Gluconobacter oxydans 621H. Putative outer membrane protein. n.d.. GOX2487. Gluconobacter oxydans 621H. Outer membrane protein ...
131.130.66.201/pcomp/browse.asp?clusterid=28

*  pCOMP - Predicted Chlamydia Outer Membrane Proteins

Gluconobacter oxydans 621H. Outer membrane protein. n.d.. GFO_0212. Gramella forsetii KT0803. surface antigen D15 family outer ...
131.130.66.201/pcomp/browse.asp?clusterid=18

*  The Yeasties, The Yeasties - The WILD Beasties in my Beer! - I Think About Beer

Acetobacter, Gluconobacter, and Gluconacetobacterare common Acetic Acid Bacteria that are used in vinegar production. These are ...
https://ithinkaboutbeer.com/2012/07/13/the-yeasties-the-yeasties-the-wild-beasties-in-my-beer/

*  A design-build-test cycle using modeling and experiments reveals interdependencies between upper glycolysis and xylose uptake...

Capillary electrophoresis for the monitoring of carboxylic acid production by Gluconobacter oxydans. J Chromatogr A. 2010;1217( ...
https://biotechnologyforbiofuels.biomedcentral.com/articles/10.1186/s13068-017-0838-5

*  Kegg pathway models for JSim

Gluconobacter oxydans. SBML. MML. gsu00941. Geobacter sulfurreducens. SBML. MML. gur00941. Geobacter uraniumreducens. SBML. MML ...
nsr.bioeng.washington.edu/jsim/models/kegg/pathway.html?00941

*  Kegg pathway models for JSim

Gluconobacter oxydans. SBML. MML. gur00631. Geobacter uraniumreducens. SBML. MML. har00631. Herminiimonas arsenicoxydans. SBML ...
nsr.bioeng.washington.edu/jsim/models/kegg/pathway.html?00631

*  高超 - 微生物学 - 人事师资 -山东大学生命

Utilization of D-lactate as an energy source supports the growth of Gluconobacter oxydans, Appl Environ Microbiol. 2015, 81, ... 3-butanediol into acetoin using Gluconobacter oxydans DSM 2003, Biotechnol Biofuels, 2013, 6, 155, SCI, IF= 7.398 ... 2-hydroxybutyric acid using whole cells of Gluconobacter oxydans, Bioresour Technol, 2012, 115, SCI, IF=5.33 ...
lifesci.sdu.edu.cn/showContent.aspx?id=1088

*  Sesura Beauty for Women | The best prices online in Philippines | iPrice

... gluconobacter/honey ferment filtrate, hematite extract (obsidian), tranexamic acid. How to Use: 1. Cleanse the skin. 2. Apply ...
https://iprice.ph/sesura-beauty/women/

Adolf Karl Ludwig ClausPseudomonadaceae: Pseudomonadaceae is a family of bacteria that includes the genera Azomonas, Azomonotrichon, Azorhizophilus, Azotobacter, Cellvibrio, Mesophilobacter, Pseudomonas (the type genus), Rhizobacter, Rugamonas, and Serpens.Skerman, McGowan and Sneath (editors): Approved Lists of Bacterial Names.Acidomonas: Acidomonas is a genus in the phylum Proteobacteria (Bacteria). The genus contains single species, namely A.SorboseSorbitol dehydrogenase: Sorbitol dehydrogenase (or SDH) is a cytosolic enzyme. In humans this protein is encoded by the SORD gene.Sobrietol: Sobrietol is a North American brand of nutritional supplement marketed as a remedy for hangovers and to prevent symptoms associated with alcohol flush reaction. The list of ingredients includes the enzymes quinoptotein alcohol dehydrogenase (QADH) and quinoprotein aldehyde dehydrogenase (QALDH) from Glucanobacter suboxydans or Acetobacter suboxydans or oxydans, either in purified form or as cell extracts, together with buffering agents and protectants designed to ensure that the enzymes remain biologically active after oral ingestion, and "a source of oxygen in an amount sufficient for the enzymes to metabolize ethanol after administration to a patient.Aldonic acidDihydroxyacetonePyrroloquinoline quinoneD-arabitol-phosphate dehydrogenase: D-arabitol-phosphate dehydrogenase (, APDH, D-arabitol 1-phosphate dehydrogenase, D-arabitol 5-phosphate dehydrogenase) is an enzyme with system name D-arabitol-phosphate:NAD+ oxidoreductase. This enzyme catalyses the following chemical reactionPentosuriaAcetic acid bacteria: Acetic acid bacteria (AAB) derive their energy from the oxidation of ethanol to acetic acid during fermentation. They are gram-negative, aerobic, rod-shaped bacteria.XylitolGlyceric acidSoluble quinoprotein glucose dehydrogenase: Soluble quinoprotein glucose dehydrogenase (, soluble glucose dehydrogenase, sGDH, glucose dehydrogenase (PQQ-dependent)) is an enzyme with system name D-glucose:acceptor oxidoreductase. This enzyme catalyses the following chemical reactionCommunity Fingerprinting: Community fingerprinting refers to a set of molecular biology techniques that can be used to quickly profile the diversity of a microbial community. Rather than directly identifying or counting individual cells in an environmental sample, these techniques show how many variants of a gene are present.RibitolShikimic acidPelagibacter ubique: Pelagibacter, with the single species P. ubique, was isolated in 2002 and given a specific name, although it has not yet been validly published according to the bacteriological code.Ketose: A ketose is a monosaccharide containing one ketone group per molecule.SaccharolipidNADH:ubiquinone reductase (non-electrogenic): NADH:ubiquinone reductase (non-electrogenic) (, ubiquinone reductase, coenzyme Q reductase, dihydronicotinamide adenine dinucleotide-coenzyme Q reductase, DPNH-coenzyme Q reductase, DPNH-ubiquinone reductase, NADH-coenzyme Q oxidoreductase, NADH-coenzyme Q reductase, NADH-CoQ oxidoreductase, NADH-CoQ reductase) is an enzyme with system name NADH:ubiquinone oxidoreductase. This enzyme catalyses the following chemical reactionAlcohol dehydrogenaseGlycerol 3-phosphate: -glycerol 1-phosphate-glycerol 3-phosphate-α-glycerophosphate-α-phosphoglycerol

(1/50) Isolation and characterization of thermotolerant Gluconobacter strains catalyzing oxidative fermentation at higher temperatures.

Thermotolerant acetic acid bacteria belonging to the genus Gluconobacter were isolated from various kinds of fruits and flowers from Thailand and Japan. The screening strategy was built up to exclude Acetobacter strains by adding gluconic acid to a culture medium in the presence of 1% D-sorbitol or 1% D-mannitol. Eight strains of thermotolerant Gluconobacter were isolated and screened for D-fructose and L-sorbose production. They grew at wide range of temperatures from 10 degrees C to 37 degrees C and had average optimum growth temperature between 30-33 degrees C. All strains were able to produce L-sorbose and D-fructose at higher temperatures such as 37 degrees C. The 16S rRNA sequences analysis showed that the isolated strains were almost identical to G. frateurii with scores of 99.36-99.79%. Among these eight strains, especially strains CHM16 and CHM54 had high oxidase activity for D-mannitol and D-sorbitol, converting it to D-fructose and L-sorbose at 37 degrees C, respectively. Sugar alcohols oxidation proceeded without a lag time, but Gluconobacter frateurii IFO 3264T was unable to do such fermentation at 37 degrees C. Fermentation efficiency and fermentation rate of the strains CHM16 and CHM54 were quite high and they rapidly oxidized D-mannitol and D-sorbitol to D-fructose and L-sorbose at almost 100% within 24 h at 30 degrees C. Even oxidative fermentation of D-fructose done at 37 degrees C, the strain CHM16 still accumulated D-fructose at 80% within 24 h. The efficiency of L-sorbose fermentation by the strain CHM54 at 37 degrees C was superior to that observed at 30 degrees C. Thus, the eight strains were finally classified as thermotolerant members of G. frateurii.  (+info)

(2/50) Membrane-bound sugar alcohol dehydrogenase in acetic acid bacteria catalyzes L-ribulose formation and NAD-dependent ribitol dehydrogenase is independent of the oxidative fermentation.

To identify the enzyme responsible for pentitol oxidation by acetic acid bacteria, two different ribitol oxidizing enzymes, one in the cytosolic fraction of NAD(P)-dependent and the other in the membrane fraction of NAD(P)-independent enzymes, were examined with respect to oxidative fermentation. The cytoplasmic NAD-dependent ribitol dehydrogenase (EC 1.1.1.56) was crystallized from Gluconobacter suboxydans IFO 12528 and found to be an enzyme having 100 kDa of molecular mass and 5 s as the sedimentation constant, composed of four identical subunits of 25 kDa. The enzyme catalyzed a shuttle reversible oxidoreduction between ribitol and D-ribulose in the presence of NAD and NADH, respectively. Xylitol and L-arabitol were well oxidized by the enzyme with reaction rates comparable to ribitol oxidation. D-Ribulose, L-ribulose, and L-xylulose were well reduced by the enzyme in the presence of NADH as cosubstrates. The optimum pH of pentitol oxidation was found at alkaline pH such as 9.5-10.5 and ketopentose reduction was found at pH 6.0. NAD-Dependent ribitol dehydrogenase seemed to be specific to oxidoreduction between pentitols and ketopentoses and D-sorbitol and D-mannitol were not oxidized by this enzyme. However, no D-ribulose accumulation was observed outside the cells during the growth of the organism on ribitol. L-Ribulose was accumulated in the culture medium instead, as the direct oxidation product catalyzed by a membrane-bound NAD(P)-independent ribitol dehydrogenase. Thus, the physiological role of NAD-dependent ribitol dehydrogenase was accounted to catalyze ribitol oxidation to D-ribulose in cytoplasm, taking D-ribulose to the pentose phosphate pathway after being phosphorylated. L-Ribulose outside the cells would be incorporated into the cytoplasm in several ways when need for carbon and energy sources made it necessary to use L-ribulose for their survival. From a series of simple experiments, membrane-bound sugar alcohol dehydrogenase was concluded to be the enzyme responsible for L-ribulose production in oxidative fermentation by acetic acid bacteria.  (+info)

(3/50) NADPH-dependent L-sorbose reductase is responsible for L-sorbose assimilation in Gluconobacter suboxydans IFO 3291.

The NADPH-dependent L-sorbose reductase (SR) of L-sorbose-producing Gluconobacter suboxydans IFO 3291 contributes to intracellular L-sorbose assimilation. The gene disruptant showed no SR activity and did not assimilate the once-produced L-sorbose, indicating that the SR functions mainly as an L-sorbose-reducing enzyme in vivo and not as a D-sorbitol-oxidizing enzyme.  (+info)

(4/50) Membrane-bound quinoprotein D-arabitol dehydrogenase of Gluconobacter suboxydans IFO 3257: a versatile enzyme for the oxidative fermentation of various ketoses.

Solubilization of membrane-bound quinoprotein D-arabitol dehydrogenase (ARDH) was done successfully with the membrane fraction of Gluconobacter suboxydans IFO 3257. In enzyme solubilization and subsequent enzyme purification steps, special care was taken to purify ARDH as active as it was in the native membrane, after many disappointing trials. Selection of the best detergent, keeping ARDH as the holoenzyme by the addition of PQQ and Ca2+, and of a buffer system involving acetate buffer supplemented with Ca2+, were essential to treat the highly hydrophobic and thus labile enzyme. Purification of the enzyme was done by two steps of column chromatography on DEAE-Toyopearl and CM-Toyopearl in the presence of detergent and Ca2+. ARDH was homogenous and showed a single sedimentation peak in analytical ultracentrifugation. ARDH was dissociated into two different subunits upon SDS-PAGE with molecular masses of 82 kDa (subunit I) and 14 kDa (subunit II), forming a heterodimeric structure. ARDH was proven to be a quinoprotein by detecting a liberated PQQ from SDS-treated ARDH in HPLC chromatography. More preliminarily, an EDTA-treated membrane fraction lost the enzyme activity and ARDH activity was restored to the original level by the addition of PQQ and Ca2+. The most predominant unique character of ARDH, the substrate specificity, was highly versatile and many kinds of substrates were oxidized irreversibly by ARDH, not only pentitols but also other polyhydroxy alcohols including D-sorbitol, D-mannitol, glycerol, meso-erythritol, and 2,3-butanediol. ARDH may have its primary function in the oxidative fermentation of ketose production by acetic acid bacteria. ARDH contained no heme component, unlike the type II or type III quinoprotein alcohol dehydrogenase (ADH) and did not react with primary alcohols.  (+info)

(5/50) Purification and characterization of membrane-bound quinoprotein cyclic alcohol dehydrogenase from Gluconobacter frateurii CHM 9.

A quinoprotein catalyzing oxidation of cyclic alcohols was found in the membrane fraction for the first time, after extensive screening among aerobic bacteria. Gluconobacter frateurii CHM 9 was finally selected in this study. The enzyme tentatively named membrane-bound cyclic alcohol dehydrogenase (MCAD) was found to occur specifically in the membrane fraction, and pyrroloquinoline quinone (PQQ) was functional as the primary coenzyme in the enzyme activity. MCAD catalyzed only oxidation reaction of cyclic alcohols irreversibly to corresponding ketones. Unlike already known cytosolic NAD(P)H-dependent alcohol-aldehyde or alcohol-ketone oxidoreductases, MCAD was unable to catalyze the reverse reaction of cyclic ketones or aldehydes to cyclic alcohols. MCAD was solubilized and purified from the membrane fraction of the organism to homogeneity. Differential solubilization to eliminate the predominant quinoprotein alcohol dehydrogenase (ADH), and the subsequent two steps of column chromatographies, brought MCAD to homogeneity. Purified MCAD had a molecular mass of 83 kDa by SDS-PAGE. Substrate specificity showed that MCAD was an enzyme oxidizing a wide variety of cyclic alcohols. Some minor enzyme activity was found with aliphatic secondary alcohols and sugar alcohols, but not primary alcohols, differentiating MCAD from quinoprotein ADH. NAD-dependent cytosolic cyclic alcohol dehydrogenase (CCAD) in the same organism was crystallized and its catalytic and physicochemical properties were characterized. Judging from the catalytic properties of CCAD, it was apparent that CCAD was distinct from MCAD in many respects and seemed to make no contributions to cyclic alcohol oxidation.  (+info)

(6/50) Purification and properties of membrane-bound D-sorbitol dehydrogenase from Gluconobacter suboxydans IFO 3255.

D-Sorbitol dehydrogenase was solubilized from the membrane fraction of Gluconobacter suboxydans IFO 3255 with Triton X-100 in the presence of D-sorbitol. Purification of the enzyme was done by fractionation with column chromatographies of DEAE-Cellulose, DEAE-Sepharose, hydroxylapatite, and Sephacryl HR300 in the presence of Triton X-100. The molecular mass of the enzyme was 800 kDa, consisting of homologous subunits of 80 kDa. The optimum pH of the enzyme activity was 6.0, and the optimum temperature was 30 degrees C. Western blot analysis suggested the occurrence of the enzyme in all the Gluconobacter strains tested.  (+info)

(7/50) Molecular cloning and functional expression of D-sorbitol dehydrogenase from Gluconobacter suboxydans IF03255, which requires pyrroloquinoline quinone and hydrophobic protein SldB for activity development in E. coli.

The sldA gene that encodes the D-sorbitol dehydrogenase (SLDH) from Gluconobacter suboxydans IFO 3255 was cloned and sequenced. It encodes a polypeptide of 740 residues, which contains a signal sequence of 24 residues. SLDH had 35-37% identity to the membrane-bound quinoprotein glucose dehydrogenases (GDHs) from E. coli, Gluconobacter oxydans, and Acinetobacter calcoaceticus except the N-terminal hydrophobic region of GDH. Additionally, the sldB gene located just upstream of sldA was found to encode a polypeptide consisting of 126 very hydrophobic residues that is similar in sequence to the one-sixth N-terminal region of the GDH. For the development of the SLDH activity in E. coli, co-expression of the sldA and sldB genes and the presence of pyrrloquinolone quinone as a co-factor were required.  (+info)

(8/50) Gluconobacter asaii Mason and Claus 1989 is a junior subjective synonym of Gluconobacter cerinus Yamada and Akita 1984.

Five strains received as Gluconobacter cerinus and Gluconobacter asaii were examined for DNA base composition, DNA-DNA similarity, 16S rRNA gene sequences and phenotypic characteristics, including acid production from ethanol, growth on L-arabitol and meso-ribitol and requirement for nicotinic acid. The five strains showed DNA base compositions ranging from 54 to 56 mol% G+C. G. cerinus IFO 3267T and IAM 1832 and G. asaii IFO 3276T and IFO 3275 showed high levels of DNA-DNA similarity (70-100%) between each other and low values of DNA-DNA similarity (16-35%) to Gluconobacter frateurii IFO 3264T and Gluconobacter oxydans IFO 14819T. G. cerinus IFO 3267T and G. asaii IFO 3276T were located at an identical position in a phylogenetic tree deduced from 16S rRNA gene sequences. Two G. cerinus strains and two G. asaii strains did not require nicotinic acid for growth and did not grow on L-arabitol or meso-ribitol. G. cerinus IAM 1832 did not produce acid and required nicotinic acid and/or other growth factors. G. asaii IFO 3265 showed a high degree of DNA-DNA similarity (97%) to G. frateurii IFO 3264T and low similarity values (each 32%) to G. cerinus IFO 3267T and G. asaii IFO 3276T. This strain did not require nicotinic acid and grew well on L-arabitol and meso-ribitol. Therefore, G. asaii IFO 3265 was reclassified as G. frateurii. The results obtained revealed a synonymous relationship between G. cerinus and G. asaii. G. asaii is a junior subjective synonym of G. cerinus because G. cerinus has priority over G. asaii.  (+info)



acetic acid bacterium


  • RT "Complete genome sequence of the acetic acid bacterium Gluconobacter RT oxydans. (genome.jp)

621H


  • OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans). (genome.jp)