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John Cullum - One of the best experts on this subject based on the ideXlab platform.

  • The pyrroloquinoline quinone synthesis genes of Gluconobacter Oxydans.
    FEMS Microbiology Letters, 2000
    Co-Authors: Marius Felder, Ghulam Nabi Qazi, Arun Gupta, Vijeshwar Verma, Anil Kumar, John Cullum
    Abstract:

    A Tn5-induced glucose dehydrogenase (GDH) deficient mutant of Gluconobacter Oxydans IFO 3293 was characterised. DNA sequencing showed that the insertion site occurred in an open reading frame with homology to the pqqE gene. It was shown that acid production could be restored by addition of the coenzyme pyrroloquinoline quinone (PQQ) to the medium. The pqq cluster of G. Oxydans ATCC 9937 was cloned and sequenced. It has five genes pqqA–E. The cluster could complement the Tn5-induced mutation in IFO 3293. Pulsed-field gel electrophoresis suggested that the pqq genes are not closely linked to the ribF gene that produces the riboflavin cofactor for the gluconic acid dehydrogenase.

  • A mutant of Gluconobacter Oxydans deficient in gluconic acid dehydrogenase
    FEMS microbiology letters, 1999
    Co-Authors: Arun Gupta, Vijeshwar Verma, Marius Felder, John Cullum, Gulam Nabi Qazi
    Abstract:

    Gluconobacter Oxydans ATCC 9937 was subjected to transposon mutagenesis using Tn5. A non-pigmented mutant was shown to be defective in gluconic acid dehydrogenase and to produce gluconic acid from glucose, whereas the parent strain produced 2,5-diketogluconic acid. Cloning and sequencing of the region containing the Tn5 insertion showed that the insertion point occurred in an open reading frame homologous (42% amino acid identity) to the ribF genes of Pseudomonas fluorescens and Escherichia coli. The resulting lack of a riboflavin cofactor would explain the loss of enzyme activity.

  • Characterisation of plasmids from diketogluconic acid producing strains of Gluconobacter Oxydans
    Journal of biotechnology, 1994
    Co-Authors: Vijeshwar Verma, Marius Felder, John Cullum, G.n. Qazi
    Abstract:

    Gluconobacter Oxydans ATCC 9937, which produces 2,5-diketogluconic acid, an intermediate in vitamin C synthesis, has three plasmids of sizes 27.7 kb (pVJ1), 12.3 kb (pVJ2) and 18 kb (pVJ4). A restriction map was constructed of pVJ1. A potential glucose dehydrogenase gene was located on pVJ1 using the polymerase chain reaction with heterologous primers. Two other G. Oxydans strains had no detectable plasmid DNA (IFO 12258) and a plasmid (pVJ3) of 9.4 kb (IFO 3293), respectively.

Xuepeng Yang - One of the best experts on this subject based on the ideXlab platform.

Marius Felder - One of the best experts on this subject based on the ideXlab platform.

  • The pyrroloquinoline quinone synthesis genes of Gluconobacter Oxydans.
    FEMS Microbiology Letters, 2000
    Co-Authors: Marius Felder, Ghulam Nabi Qazi, Arun Gupta, Vijeshwar Verma, Anil Kumar, John Cullum
    Abstract:

    A Tn5-induced glucose dehydrogenase (GDH) deficient mutant of Gluconobacter Oxydans IFO 3293 was characterised. DNA sequencing showed that the insertion site occurred in an open reading frame with homology to the pqqE gene. It was shown that acid production could be restored by addition of the coenzyme pyrroloquinoline quinone (PQQ) to the medium. The pqq cluster of G. Oxydans ATCC 9937 was cloned and sequenced. It has five genes pqqA–E. The cluster could complement the Tn5-induced mutation in IFO 3293. Pulsed-field gel electrophoresis suggested that the pqq genes are not closely linked to the ribF gene that produces the riboflavin cofactor for the gluconic acid dehydrogenase.

  • A mutant of Gluconobacter Oxydans deficient in gluconic acid dehydrogenase
    FEMS microbiology letters, 1999
    Co-Authors: Arun Gupta, Vijeshwar Verma, Marius Felder, John Cullum, Gulam Nabi Qazi
    Abstract:

    Gluconobacter Oxydans ATCC 9937 was subjected to transposon mutagenesis using Tn5. A non-pigmented mutant was shown to be defective in gluconic acid dehydrogenase and to produce gluconic acid from glucose, whereas the parent strain produced 2,5-diketogluconic acid. Cloning and sequencing of the region containing the Tn5 insertion showed that the insertion point occurred in an open reading frame homologous (42% amino acid identity) to the ribF genes of Pseudomonas fluorescens and Escherichia coli. The resulting lack of a riboflavin cofactor would explain the loss of enzyme activity.

  • Characterisation of plasmids from diketogluconic acid producing strains of Gluconobacter Oxydans
    Journal of biotechnology, 1994
    Co-Authors: Vijeshwar Verma, Marius Felder, John Cullum, G.n. Qazi
    Abstract:

    Gluconobacter Oxydans ATCC 9937, which produces 2,5-diketogluconic acid, an intermediate in vitamin C synthesis, has three plasmids of sizes 27.7 kb (pVJ1), 12.3 kb (pVJ2) and 18 kb (pVJ4). A restriction map was constructed of pVJ1. A potential glucose dehydrogenase gene was located on pVJ1 using the polymerase chain reaction with heterologous primers. Two other G. Oxydans strains had no detectable plasmid DNA (IFO 12258) and a plasmid (pVJ3) of 9.4 kb (IFO 3293), respectively.

Vijeshwar Verma - One of the best experts on this subject based on the ideXlab platform.

  • The pyrroloquinoline quinone synthesis genes of Gluconobacter Oxydans.
    FEMS Microbiology Letters, 2000
    Co-Authors: Marius Felder, Ghulam Nabi Qazi, Arun Gupta, Vijeshwar Verma, Anil Kumar, John Cullum
    Abstract:

    A Tn5-induced glucose dehydrogenase (GDH) deficient mutant of Gluconobacter Oxydans IFO 3293 was characterised. DNA sequencing showed that the insertion site occurred in an open reading frame with homology to the pqqE gene. It was shown that acid production could be restored by addition of the coenzyme pyrroloquinoline quinone (PQQ) to the medium. The pqq cluster of G. Oxydans ATCC 9937 was cloned and sequenced. It has five genes pqqA–E. The cluster could complement the Tn5-induced mutation in IFO 3293. Pulsed-field gel electrophoresis suggested that the pqq genes are not closely linked to the ribF gene that produces the riboflavin cofactor for the gluconic acid dehydrogenase.

  • A mutant of Gluconobacter Oxydans deficient in gluconic acid dehydrogenase
    FEMS microbiology letters, 1999
    Co-Authors: Arun Gupta, Vijeshwar Verma, Marius Felder, John Cullum, Gulam Nabi Qazi
    Abstract:

    Gluconobacter Oxydans ATCC 9937 was subjected to transposon mutagenesis using Tn5. A non-pigmented mutant was shown to be defective in gluconic acid dehydrogenase and to produce gluconic acid from glucose, whereas the parent strain produced 2,5-diketogluconic acid. Cloning and sequencing of the region containing the Tn5 insertion showed that the insertion point occurred in an open reading frame homologous (42% amino acid identity) to the ribF genes of Pseudomonas fluorescens and Escherichia coli. The resulting lack of a riboflavin cofactor would explain the loss of enzyme activity.

  • Characterisation of plasmids from diketogluconic acid producing strains of Gluconobacter Oxydans
    Journal of biotechnology, 1994
    Co-Authors: Vijeshwar Verma, Marius Felder, John Cullum, G.n. Qazi
    Abstract:

    Gluconobacter Oxydans ATCC 9937, which produces 2,5-diketogluconic acid, an intermediate in vitamin C synthesis, has three plasmids of sizes 27.7 kb (pVJ1), 12.3 kb (pVJ2) and 18 kb (pVJ4). A restriction map was constructed of pVJ1. A potential glucose dehydrogenase gene was located on pVJ1 using the polymerase chain reaction with heterologous primers. Two other G. Oxydans strains had no detectable plasmid DNA (IFO 12258) and a plasmid (pVJ3) of 9.4 kb (IFO 3293), respectively.

  • Intergeneric protoplast fusion between Gluconobacter Oxydans and Corynebacterium species.
    Journal of biotechnology, 1992
    Co-Authors: Vijeshwar Verma, Ghulam Nabi Qazi, Rajinder Parshad
    Abstract:

    Abstract Intergeneric protoplast fusion between 2,5-diketo-gluconic acid producing Gluconobacter Oxydans (ATCC 9937) and a mutant strain of Corynebacterium species (ATCC 31090), capable of reducing 2,5-diketo-gluconic acid to 2-keto- l -gulonic acid, a penultimate step in vitamin C production) resulted in viable recombinants. Some of the fusion products exhibited the capacity to convert d -glucose to 2-keto- l -gulonic acid, but the conversion rate is low.

  • Diketo-gluconate fermentation by Gluconobacter Oxydans
    Enzyme and Microbial Technology, 1991
    Co-Authors: Ghulam Nabi Qazi, Rajinder Parshad, Vijeshwar Verma, C.l. Chopra, R. Buse, Michael Träger, Ulfert Onken
    Abstract:

    Abstract Production of 2,5-diketogluconate by Gluconobacter Oxydans (ATCC9937) in two types of reactors, namely, airlift and stirred fermentors, is described. Accumulation of diketo-acid is shown to be dependent on the pH of the medium. Oxidation of gluconate to 2,5-diketogluconate in Gluconobacter Oxydans is described as a specific reaction carried out through an intermediate of 2-ketogluconate rather than 5-ketogluconate. The enzyme profile of the culture depicting two distinct phases, i.e. direct glucose oxidation and gluconate oxidation, is described.

Dongzhi Wei - One of the best experts on this subject based on the ideXlab platform.

  • Effective improvement of the activity of membrane-bound alcohol dehydrogenase by overexpression of adhS in Gluconobacter Oxydans
    Biotechnology letters, 2016
    Co-Authors: Huan Zhang, Jinping Lin, Ming Sun, Lulu Shi, Dongzhi Wei
    Abstract:

    Objectives To investigate the roles of adhS, which encodes the AdhS subunit of membrane-bound alcohol dehydrogenase (mADH) in Gluconobacter Oxydans DSM2003, and to rationally improve mADH activity.

  • Phosphorylation of HPr by HPr Kinase in Gluconobacter Oxydans 621H
    Protein and peptide letters, 2014
    Co-Authors: Ping Zhang, Fengqing Wang, Dongzhi Wei
    Abstract:

    DNA sequencing has revealed that Gluconobacter Oxydans may contain an incomplete phosphoenolpyruvate: carbohydrate phosphotransferase system (PTS), but the function of individual members of the system remains unknown. Here we demonstrated that the predicted histidine protein HPr, an essential component of PTS, can be phosphorylated by a predicted HPr kinase in G. Oxydans, where Ser54 in HPr is the site responsible for such a phosphorylation. The discovery implies that G. Oxydans may regulate PTS activity in a way similar to that identified in some Gram-positive bacteria with low GC content.

  • Immobilization of Gluconobacter Oxydans by Entrapment in Porous Chitosan Sponge
    Journal of bioprocessing & biotechniques, 2013
    Co-Authors: Cunxun Wang, Dongzhi Wei, Xu Zhou, Yuhong Ren
    Abstract:

    The porous chitosan sponge was prepared using NaHCO3 as the porogen and used to immobilize Gluconobacter Oxydans. Under the optimum conditions, the activity recovery of the immobilized cells reached 92%. The morphology characterization of the immobilized cells revealed that the cells were attached to the surface of the pores (100-400μm) which were well distributed in the chitosan sponge. The valuation of cell activity showed that the immobilized cells displayed enhanced pH and thermal stability compared to free cells. Furthermore, the immobilized cells retained 74% of its origin activity after 12 repeated reaction cycles separated by filtration.

  • Characterization of a novel dextran produced by Gluconobacter Oxydans DSM 2003.
    Applied microbiology and biotechnology, 2011
    Co-Authors: Shu Wang, Jinping Lin, Xiangzhao Mao, Hualei Wang, Dongzhi Wei
    Abstract:

    A novel water-soluble dextran was synthesized from maltodextrin by cell-free extract of Gluconobacter Oxydans DSM 2003. The dextran was purified by size exclusion chromatography, and the structure was determined by Fourier transform infrared spectroscopy, nuclear magnetic resonance, and gas chromatography–mass spectrometer. Based on the spectral data, we found that the dextran contained only d-glucose residues. The ratio of nonreducing end glucopyranosyl (Glcp) to 6-linked Glcp to 4,6-linked Glcp was estimated to be 8.62:78.79:12.59 by methylation analysis. This result indicated the existence of a small proportion of α(1,4) branches in α(1,6) glucosyl linear chains. Here, we reported the first time a novel dextran was synthesized by G. Oxydans DSM 2003.

  • Highly Selective Oxidation of Benzyl Alcohol Using Engineered Gluconobacter Oxydans in Biphasic System
    Current microbiology, 2010
    Co-Authors: Jinping Lin, Dongzhi Wei
    Abstract:

    The Gluconobacter Oxydans M5 with disruption of the pyrroloquinoline quinine-dependent membrane-bound aldehyde dehydrogenase (ALDH) was used for the oxidation of benzyl alcohol. The selectivity toward benzaldehyde showed an obvious increase for the engineered strain, which reached the 67.3%, while the wild strain had only 2.8%. Meantime, the aqueous/isooctane (1:1) biphasic system was used for the further improvement of selectivity. By these methods, nearly 100% selectivity and conversion rate could be obtained within 1 h at the optimum initial benzyl alcohol concentration of 5.0 g/l.