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  • 1
    Electronic Resource
    Electronic Resource
    Increase in glucan formation by Botrytis cinerea and analysis of the adherent glucan (1990)
    Springer
    Applied microbiology and biotechnology 33 (1990), S. 1-6 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Glucan production by Botrytis cinerea increased from 1 g/l to 3 g/l when KNO3 or urea replaced asparagine as the nitrogen source. A further enhancement up to 5 g/l was obtained with nitrogen-limited medium or non-growing cells. Under these conditions an extracellular glucan layer was attached to the mycelium. The adherent glucan made up 60% of the total amount of glucan produced and thus increased the total glucan yield to 13 g/l. An enzymatic analysis of the adherent glucan indicated that only about every fifth molecule of the main chain was substituted by a glucose unit. In contrast, in the free glucan of culture filtrates glucose units were distributed at approximately every second to third residue of the main chain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00170559
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Electron transport chain of Zymomonas mobilis (1990)
    Springer
    Archives of microbiology 154 (1990), S. 536-543 
    Details
    ISSN: 1432-072X
    Keywords: Zymomonas mobilis ; Glucose dehydrogenase ; Pyrroloquinoline quinone ; Ubiquinone ; Electron transport chain ; TMPD oxidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The interaction of the membrane-bound glucose dehydrogenase from the anaerobic but aerotolerant bacterium Zymomonas mobilis with components of the electron transport chain has been studied. Cytoplasmic membranes showed reduction of oxygen to water with the substrates glucose or NADH. The effects of the respiratory chain inhibitors piericidin, capsaicin, rotenone, antimycin, myxothiazol, HQNO, and stigmatellin on the oxygen comsumption rates in the presence of NADH or glucose as substrates indicated that a complete and in the most parts identical respiratory chain is participating in the glucose as well as in the NADH oxidation. Furthermore, the presence of coenzyme Q10 (ubiquinone 10) in Z. mobilis was demonstrated. Extraction from and reincorporation of the quinone into the membranes revealed that ubiquinone is essential for the respiratory activity with glucose and NADH. In addition, a membrane-associated tetramethyl-p-phenylene-diamine-oxidase activity could be detected in Z. mobilis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00248833
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Cloning the dapA dapB cluster of the lysine-secreting bacterium Corynebacterium glutamicum (1990)
    Springer
    Molecular genetics and genomics 220 (1990), S. 478-480 
    Details
    ISSN: 1617-4623
    Keywords: Corynebacterium glutamicum ; Lysine biosynthesis ; Dihydrodipicolinate synthase ; Dihydrodipicolinate reductase ; Cluster formation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The genes encoding the two successive enzymes of the lysine biosynthetic pathway, dihydrodipicolinate synthase (dapA) and dihydrodipicolinate reductase (dapB), have been isolated from Corynebacterium glutamicum by heterologous complementation of Escherichia coli mutants. The two genes reside on a single 3.8-kb chromosomal fragment. They were subcloned as non overlapping fragments on an E. coli/C. glutamicum shuttle vector and introduced into C. glutamicum. This resulted in overexpression of both enzyme activities which was irrespective of the orientation of the inserts and comparable to that obtained with the large 3.8-kb fragment. Therefore, both genes are located in close proximity to each other on the C. glutamicum chromosome, but are apparently independently transcribed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00391757
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  • 4
    Electronic Resource
    Electronic Resource
    Construction of expression vectors for the gram-negative bacterium Zymomonas mobilis (1990)
    Springer
    Molecular genetics and genomics 223 (1990), S. 335-341 
    Details
    ISSN: 1617-4623
    Keywords: Pyruvate decarboxylase gene (pdc) ; Expression vectors ; Promoter/terminator ; Chloramphenicol acetyltransferase ; Zymomonas mobilis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A set of vectors was constructed for the cloning and expression of heterologous genes in the Gramnegative bacterium Zymomonas mobilis under the control of the pdc promoter of Z. mobilis. The vectors pPTZ1, pPTZ3, and pPTZ4 are based on the cryptic Z. mobilis plasmid pZM02 and on parts of the Escherichia coli plasmids pKK223-3 and pBR322 together with the multiple cloning site of phage Ml3mp18. DNA fragments can be readily inserted immediately downstream from the pdc promoter at unique restriction sites for KpnI, XbaI and PstI in pPTZl and additionally for SmaI and BamHI in pPTZ3. In pPTZ4, the 5′ terminal codons of pdc were deleted allowing the formation of gene fusions. Expression of a promoterless chloramphenicol acetyltransferase gene (cat) controlled by the pdc gene promoter resulted in enzyme activities of up to 5.5 U/mg total cell protein in Z. mobilis cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00265073
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    Paper (German National Licenses)
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