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  • American Society for Microbiology  (3)
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  • American Society for Microbiology  (3)
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  • 1
    Online-Ressource
    Online-Ressource
    Cloning of the xynB Gene from Dictyoglomus thermophilum Rt46B.1 and Action of the Gene Product on Kraft Pulp
    American Society for Microbiology ; 1998
    In:  Applied and Environmental Microbiology Vol. 64, No. 5 ( 1998-05), p. 1759-1765
    Details
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 64, No. 5 ( 1998-05), p. 1759-1765
    Kurzfassung: A two-step PCR protocol was used to identify and sequence a family 11 xylanase gene from Dictyoglomus thermophilum Rt46B.1. Family 11 xylanase consensus fragments (GXCFs) were amplified from Rt46B.1 genomic DNA by using different sets of consensus PCR primers that exhibited broad specificity for conserved motifs within fungal and/or bacterial family 11 xylanase genes. On the basis of the sequences of a representative sample of the GXCFs a single family 11 xylanase gene ( xynB ) was identified. The entire gene sequence was obtained in the second step by using genomic walking PCR to amplify Rt46B.1 genomic DNA fragments upstream and downstream of the xynB GXCF region. The putative XynB peptide ( M r , 39,800) encoded by the Rt46B.1 xynB open reading frame was a multidomain enzyme comprising an N-terminal catalytic domain ( M r , 22,000) and a possible C-terminal substrate-binding domain ( M r , 13,000) that were separated by a short serine-glycine-rich 23-amino-acid linker peptide. Seven xylanases which differed at their N and C termini were produced from different xynB expression plasmids. All seven xylanases exhibited optimum activity at pH 6.5. However, the temperature optima of the XynB xylanases varied from 70 to 85°C. Pretreatment of Pinus radiata and eucalypt kraft-oxygen pulps with XynB resulted in moderate xylan solubilization and a substantial improvement in the bleachability of these pulps.
    Materialart: Online-Ressource
    ISSN: 0099-2240 , 1098-5336
    URL: Article
    DOI: 10.1128/AEM.64.5.1759-1765.1998
    RVK:
    WA 15000
    Sprache: Englisch
    Verlag: American Society for Microbiology
    Publikationsdatum: 1998
    ZDB Id: 223011-2
    ZDB Id: 1478346-0
    SSG: 12
    Standort Signatur Einschränkungen Verfügbarkeit
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    Online-Ressource
  • 2
    Online-Ressource
    Online-Ressource
    A Gene Encoding a Novel Multidomain β-1,4-Mannanase from Caldibacillus cellulovorans and Action of the Recombinant Enzyme on Kraft Pulp
    American Society for Microbiology ; 2000
    In:  Applied and Environmental Microbiology Vol. 66, No. 2 ( 2000-02), p. 664-670
    Details
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 66, No. 2 ( 2000-02), p. 664-670
    Kurzfassung: Genomic walking PCR was used to obtained a 4,567-bp nucleotide sequence from Caldibacillus cellulovorans . Analysis of this sequence revealed that there were three open reading frames, designated ORF1, ORF2, and ORF3. Incomplete ORF1 encoded a putative C-terminal cellulose-binding domain (CBD) homologous to members of CBD family IIIb, while putative ORF3 encoded a protein of unknown function. The putative ManA protein encoded by complete manA ORF2 was an enzyme with a novel multidomain structure and was composed of four domains in the following order: a putative N-terminal domain (D1) of unknown function, an internal CBD (D2), a β-mannanase catalytic domain (D3), and a C-terminal CBD (D4). All four domains were linked via proline-threonine-rich peptides. Both of the CBDs exhibited sequence similarity to family IIIb CBDs, while the mannanase catalytic domain exhibited homology to the family 5 glycosyl hydrolases. The purified recombinant enzyme ManAd3 expressed from the cloned catalytic domain (D3) exhibited optimum activity at 85°C and pH 6.0 and was extremely thermostable at 70°C. This enzyme exhibited high specificity with the substituted galactomannan locust bean gum, while more substituted galacto- and glucomannans were poorly hydrolyzed. Preliminary studies to determine the effect of the recombinant ManAd3 and a recombinant thermostable β-xylanase on oxygen-delignified Pinus radiata kraft pulp revealed that there was an increase in the brightness of the bleached pulp.
    Materialart: Online-Ressource
    ISSN: 0099-2240 , 1098-5336
    URL: Article
    DOI: 10.1128/AEM.66.2.664-670.2000
    RVK:
    WA 15000
    Sprache: Englisch
    Verlag: American Society for Microbiology
    Publikationsdatum: 2000
    ZDB Id: 223011-2
    ZDB Id: 1478346-0
    SSG: 12
    Standort Signatur Einschränkungen Verfügbarkeit
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    Online-Ressource
  • 3
    Online-Ressource
    Online-Ressource
    In Vitro Activity of Josamycin Against Aerobic Gram-Positive Cocci and Anaerobes
    American Society for Microbiology ; 1976
    In:  Antimicrobial Agents and Chemotherapy Vol. 9, No. 6 ( 1976-06), p. 988-993
    Details
    In: Antimicrobial Agents and Chemotherapy, American Society for Microbiology, Vol. 9, No. 6 ( 1976-06), p. 988-993
    Kurzfassung: Josamycin, a new macrolide antibiotic, was compared with ampicillin, erythromycin, and clindamycin in vitro against 25 isolates each of pneumococci, enterococci, Staphylococcus aureus, S. epidermidis , and nonenterococcal hemolytic streptococci and against 25 anaerobes including 10 Bacteroides fragilis . Minimal inhibitory concentration and minimal bactericidal concentration data were obtained for the aerobic organisms, using serial twofold tube dilutions in Mueller-Hinton broth. Minimal inhibitory concentrations were determined for the anaerobes by the agar dilution technique. Josamycin was comparable to erythromycin and clindamycin in activity against the pneumococci, streptococci, and staphylococci and was more active than clindamycin against enterococci. It was somewhat less active than ampicillin against enterococci and S. epidermidis and showed its greatest in vitro activity against anaerobes, being comparable to clindamycin.
    Materialart: Online-Ressource
    ISSN: 0066-4804 , 1098-6596
    URL: Article
    DOI: 10.1128/AAC.9.6.988
    RVK:
    XA 24552
    Sprache: Englisch
    Verlag: American Society for Microbiology
    Publikationsdatum: 1976
    ZDB Id: 1496156-8
    SSG: 12
    SSG: 15,3
    Standort Signatur Einschränkungen Verfügbarkeit
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    Online-Ressource
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