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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Microbial ecology 12 (1986), S. 147-153 
    ISSN: 1432-184X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Recent microbiological findings show how compounds, regarded hitherto as unusual substrates for anaerobic bacteria, are degraded under anaerobic conditions. The complete conversion of halobenzoic acids and halophenolic compounds to methane by lake sediment and sewage sludge microorganisms has been demonstrated. Since haloaromatic compounds are widely used and may be found in such effluents as those from the forest industry, these studies could stimulate a broader interest in anaerobic treatment of industrial waste waters which contain unusual organic compounds.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-072X
    Keywords: Induction ; Carbon catabolite repression ; Alcohol oxidase ; Catalase ; Methanol ; Mixed substrates ; Continuous culture ; Hansenula polymorpha
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The regulation of the synthesis of alcohol oxidase, catalase, formaldehyde dehydrogenase and formate dehydrogenase was investigated in the methanol-utilizing yeast Hansenula polymorpha. The organism was found to synthesize immunologically identical alcohol oxidases during growth on glycerol and methanol. Growth on glycerol, however, was not dependent on the alcohol oxidase, as was shown with a mutant without alcohol oxidase protein. Similarly it was shown with a catalase activity negative mutant that high catalase activity during growth on glycerol was not a prerequisite for the utilization of this substrate, though absolutely required for growth on methanol. Experiments were conducted with mixed substrates to study the influence of methanol on alcohol oxidase synthesis. In batch cultures, growth on ribose plus methanol resulted in an enhanced rate of alcohol oxidase synthesis as compared to ribose alone. In continuous cultures, (D=0.1 h-1) addition of methanol to glycerol-, glucose-, or sorbose-limited cultures gave rise to increased alcohol oxidase activity of up to 20 U/mg, which is about by 2 times higher than the specific activity used for growth on methanol alone. The increase in specific activity of the dissimilatory enzymes on the mixed substrates is partly due to methanol per se, as was shown by a mutant unable to dissimilate or assimilate methanol.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 76 (1971), S. 223-251 
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Description / Table of Contents: Zusammenfassung Mutanten von E. coli K 12, die gegen 1 mM 5-MT resistent sind, scheiden 1,5–3 mg/l Try ins Medium aus; sie haben wahrscheinlich eine “Feedback-resistente” Anthranilatsynthetase. Eine zweite Mutation, die zur Resistenz gegen 5-FT führte, bewirkt in diesen Stämmen eine Derepression der Try-Biosynthese-Enzyme. Der Stamm FMT 1, in dem diese beiden Try-Regulations-mechanismen ausgeschaltet sind, produziert 50 mg/l Try. Es gelang nicht, die Try-Bildung des Stammes FMT 1 dadurch zu steigern, daß auch die Regulationsmechanismen der Phe- und/oder Tyr-Biosynthese, die einen gemeinsamen Grundzweig mit der Try-Synthese haben, weitgehend ausgeschaltet wurden. Phe- und/oder Tyr-auxotrophe Mutanten bilden nicht wesentlich mehr Try als der Ausgangsstamm. Bei Mutanten von all 1, die eine stark reduzierte Tryptophanase-Aktivität besitzen, kann unter den Bedingungen der katabolischen Repression kein Try-Abbau mehr nachgewiesen werden. Die Try-Ausscheidung beträgt jedoch auch dann nur 55 mg/l. Eine Veränderung der Zellpermeabilität mittels Biotin, Penicillin oder Detergenzien hat keinen wesentlichen Einfluß auf die Try-Produktion. Die Zugabe von Indol und L-Serin zum Kulturmedium führt zu einer Erhöhung der Try-Bildung beim Stamm Ind 2 bis 700 mg/l. Stämme, die durch den Besitz eines FTry-Episoms heterogenot diploid sind für das Try-Operon, synthetisieren unter günstigen Bedingungen bei Indol- und Serin-Zusatz selbst 1 g/l Indol und bilden maximal 5 g/l Try. Wird Anthranilsäure zum Kulturmedium zugegeben, so erfolgt eine Abnahme der Try-Ausscheidung um 50%, weil die Anthranilsäure sehr wahrscheinlich die Aktivität der Indol-3-glycerol-phosphat-synthetase hemmt. Es wurden einige Mutanten isoliert, die einen Teil der zugesetzten Anthranilsäure bei gleichzeitiger Zugabe von L-Serin zu Try umsetzen können.
    Notes: Summary Mutants of E. coli K 12, which are resistant to 1 mM 5-methyltryptophan, excrete 1.5–3 mg/l tryptophan into the medium; in these strains the anthranilate-synthetase is probably insensitive to the feedback-inhibition. A second mutation for resistance to 5-fluoro-tryptophan gives strains, which are derepressed in the synthesis of the enzymes of the tryptophan pathway. The feedback-resistant and derepressed mutant FMT 1 produces 50 mg/l tryptophan. It was not possible to increase the tryptophan-accumulation of the strain FMT 1 by eliminating the control mechanism of the phenylalanine and tyrosine biosynthesis. Phenylalanine and/or tyrosine requiring mutants also do not produce more tryptophan than the prototrophic strain. Mutants of all 1 having a reduced tryptophanase activity can not decompose tryptophan under conditions of catabolite repression. But the tryptophan production is nevertheless only 55 mg/l. Altering the cellular permeability induced by biotin fatty acid derivatives or penicillin does not influence the tryptophan accumulation. The addition of indole and L-serine to the culture medium increases the tryptophan production of the strain Ind 2 to 700 mg/l. Strains from Ind 2 carrying a FTryepisome in addition to the chromosomal try-operon produce by feeding indole and serine 1 g/l indole and 5 g/l tryptophan. The addition of anthranilic acid reduces the tryptophan yeild to 50%; the reason for this phenomenon may be the inhibition of the indole-3-glycerol phosphate synthetase by anthranilic acid. Some mutants were isolated, which were able to convert some of the added anthranilic acid and serine to tryptophan.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 126 (1980), S. 141-148 
    ISSN: 1432-072X
    Keywords: Coniferyl alcohol ; Veratric acid ; Demethylation ; β-Ketoadipate pathway ; Gentisale pathway ; Nocardia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Nocardia sp. DSM 1069 was grown on mineral salt media with coniferyl alcohol, 4-methoxybenzoic acid, 3-methoxybenzoic acid or veratric acid as sole sources of carbon and energy. During incubation on coniferyl alcohol, the formation of coniferyl aldehyde, ferulic acid and quantitative accumulation of vanillic acid and proteocatechuic acid could be achieved with mutants. Washed cell suspensions of N. sp. grown on 4-methoxybenzoic acid, oxidized 4-hydroxybenzoic acid and protocatechuic acid. Cells grown on veratric acid, oxidized vanillic acid, isovanillic acid, and protocatechuic acid. Cell extracts were shown to cleave protocatechuic acid by “ortho-fission”. A mutant without protocatechuate 3,4-dioxygenase activity was not influenced in its growth on 3 methoxybenzoic acid. Cell free extracts of cells grown on 3-methoxybenzoic acid were shown to catalyze the oxidation of gentisic acid (2,5-dihydroxybenzoic acid). The resulting ring cleavage product was further metabolized by a glutathione dependent reaction. The specificity of the demethylation reactions has been investigated with a mutant unable to grow on vanillic acid. This mutant was not impaired in the degradation of isovanillic acid, 4-methoxy-, or 3-methoxybenzoic acid, whereas growth of this mutant on veratric acid (3,4-dimethoxybenzoic acid) was only half as much as that of the wild type. Concomitantly with growth on veratric acid this mutant accumulated vanillic acid with a yield of about 50%. A pathway for the catabolism of coniferyl alcohol, involving oxidation and shortening of the side chain, and of 4-methoxybenzoic acid and veratric acid with protocatechuic acid as intermediate is being proposed. A second one is proposed for the degradation of 3-methoxybenzoic acid with gentisic acid as intermediate.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1432-072X
    Keywords: Acetohydroxy acid synthase ; Isoleucine synthesis ; Amino acid fermentation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract When Corynebacterium glutamicum ATCC 14310 (leu-) was cultured with 200 mg/l leucine and 150 mM α-hydroxybutyric acid the acetohydroxy acid synthase activity was increased to 0.17 U/mg as compared to 0.03 U/mg in the wildtype. This increase was a combined effect of the limiting amounts of leucine added, together with an apparent additional internal leucine/valine shortage resulting from accumulated α-ketobutyric acid (5 mM) and the kinetic characteristics of the acetohydroxy acid synthase. The increase in the specific AHAS activity by the appropriate amino acid limitation resulted in an increased isoleucine yield of 71 mmol/l as compared to 27 mmol/l obtained under non-limiting conditions.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 146 (1986), S. 105-110 
    ISSN: 1432-072X
    Keywords: Pyruvate decarboxylase ; Zymomonas mobilis ; Purification ; Molecular weight ; Isoelectric point ; Cofactor dissociation ; Immunological studies
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Pyruvate decarboxylase (EC 4.1.1.1) from the ethanol producing bacterium Zymomonas mobilis was purified to homogeneity. This enzyme is an acidic protein with an isoelectric point of 4.87 and has an apparent molecular weight of 200,000±10,000. The enzyme showed a single band in sodium dodecylsulfate gel electrophoresis with a molecular weight of 56,500±4,000 which indicated that the enzyme consists of four probably identical subunits. The dissociation of the cofactors Mg2+ and thiamine pyrophosphate at pH 8.9 resulted in a total loss of enzyme activity which could be restored to 99.5% at pH 6.0 in the presence of both cofactors. For the apoenzyme the apparent K m values for Mg2+ and thiamine pyrophosphate were determined to be 24 μM and 1.28 μM. The apparent K m value for the substrate pyruvate was 0.4 mM. Antiserum prepared against this purified pyruvate decarboxylase failed to crossreact with cell extracts of the reportedly pyruvate decarboxylase positive bacteria Sarcina ventriculi, Erwinia amylovora, or Gluconobacter oxydans, or with cell extracts of Saccharomyces cerevisiae.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 160 (1993), S. 74-79 
    ISSN: 1432-072X
    Keywords: Zymomonas mobilis ; Oxidative phosphorylation ; membrane vesicles ; ATP synthesis ; transmembrane pH gradient ; 31P-NMR ; Acetaldehyde ; Ethanol metabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The obligately fermentative aerotolerant bacterium Zymomonas mobilis was shown to possess oxidative phosphorylation activity. Increased intracellular ATP levels were observed in aerated starved cell suspension in the presence of ethanol or acetaldehyde. Ethanolconsuming Z. mobilis generated a transmembrane pH gradient. ATP synthesis in starved Z. mobilis cells could be induced by external medium acidification of 3.5–4.0 pH units. Membrane vesicles of Z. mobilis coupled ATP synthesis to NADH oxidation. ATP synthesis was sensitive to the protonophoric uncoupler CCCP both in starved cells and in membrane vesicles. The H+-ATPase inhibitor DCCD was shown to inhibit the NADH-coupled ATP synthesis in membrane vesicles. The physiological role of oxidative phosphorylation in this obligately fermentative bacterium is discussed.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Applied microbiology and biotechnology 52 (1999), S. 146-153 
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  Amino acids have been produced with the aid of microorganisms for nearly 40 years now. The economic importance of these cellular building blocks is enormous. Demand for them is rising continuously and currently more than 106 tonnes/year are required. Continual efforts to increase production performance are directed towards the microorganisms themselves, as well as towards technical improvements of the respective processes. A special position within the amino-acid-producing microorganisms is traditionally occupied by Corynebacterium glutamicum. Molecular research in conjunction with NMR studies of flux has revealed fascinating new properties of this particular organism, including the existence of a new type of exporter and reverse fluxes within the anaplerosis. The knowledge gained will enable the further improvement of production strains and furthermore extend fundamental insights into metabolite flux management within bacteria in general.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 107 (1993), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Glucose-fructose oxidoreductase (GFOR) is a periplasmic enzyme of the ethanologenic, Gram-negative bacterium Zymomonas mobilis. It contains tightly bound NADP+ as cofactor. In Z. mobilis GFOR-recombinant strains, a precursor form of GFOR was accumulated. To assay the preGFOR for its NADP(H) content and enzymatic activity, it was purified from an overproducing strain. Using SDS-PAGE, the precursor subunit size was determined to approximately 45 kDa (compared with a 40 kDa subunit size for the mature GFOR subunit). The N-terminal amino acid sequence of the precursor was determined. The N-terminal residues of the GFOR matched with the signal sequence from the DNA sequence of the gene gfo. The precursor form of GFOR was enzymatically active and contained the cofactor NADP(H).
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 84 (1991), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The enzyme glucose-fructose oxidoreductase (GFOR) from the Gram-negative ethanologenic bacterium Zymomonas mobilis was purified to homogeneity and was shown to be a tetrameric protein with a subunit size of Mr 42 500. Using immunogold-labelling in combination with electron microscopy, ultrathin sections of Z. mobilis wild type cells showed that the enzyme GFOR is located in the periplasm off the bacterial cells. Z. mobilis strains which carried the cloned gfo gene on plasmid pSUP104, had 5–6-fold increased GFOR enzyme activities. Moreover, these cells accumulated large amounts of a presumable unprocessed pre-GFOR protein (Mr 48 000).
    Type of Medium: Electronic Resource
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