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  • 1
    Electronic Resource
    Electronic Resource
    Xylanase from the psychrophilic yeast Cryptococcus adeliae (2000)
    Springer
    Extremophiles 4 (2000), S. 137-144 
    Details
    ISSN: 1433-4909
    Keywords: Key words Xylanases ; Psychrophile ; Yeast ; Molecular adaptation ; Molecular modeling
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A xylanase belonging to family 10 is produced by Cryptococcus adeliae, an Antarctic yeast that exhibits optimal growth at low temperature. The mature glycosylated xylanase secreted by C. adeliae is composed of 338 amino acid residues and 26 ± 3 osidic residues, and shares 84% identity with its mesophilic counterpart from C. albidus. The xylanase from C. adeliae is less thermostable than its mesophilic homologue when the residual activities are compared, and this difference was confirmed by differential scanning calorimetry experiments. In the range 0°–20°C, the cold-adapted xylanase displays a lower activation energy and a higher catalytic efficiency. All these observations suggest a less compact, more flexible molecular structure. Analysis of computerized molecular models built up for both psychrophilic and mesophilic xylanases indicates that the adaptation to cold consists of discrete changes in the tridimensional structure: of 53 substitutions, 22 are presumably involved in the adaptation process. These changes lead mainly to a less compact hydrophobic packing, to the loss of one salt bridge, and to a destabilization of the macrodipoles of the helices.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007920070028
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  • 2
    Electronic Resource
    Electronic Resource
    Three-dimensional structure of a thermostable bacterial cellulase (1992)
    [s.l.] : Nature Publishing Group
    Nature 357 (1992), S. 89-91 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The three-dimensional structure of endoglucanase CelD from C. thermocullum was determined by X-ray crystallography. Two forms of native CelD (crystallized with either ammonium sulphate or CaCl2) as well as that of an inhibitor (o-iodobenzyl-1-thio-/3-cellobioside)-CeID complex were ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/357089a0
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Cloning and expression of cellulase and xylanase genes in Lactobacillus plantarum (1990)
    Springer
    Applied microbiology and biotechnology 33 (1990), S. 534-541 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Eleven cellulase genes from Gram-positive bacteria were cloned in a Lactobacillus plantarum silage inoculum. Eight of these genes were expressed as active enzymes from their original promotors and translation signals. Where tested, the enzymes produced by transformed L.plantarum had the same temperature and pH optimum as enzymes produced in the original host, or in transformed Escherichia coli. Using chloramphenicol acetyltransferase as a cell-internal marker enzyme, it could be demonstrated that at least endoglucanase D from Clostridium thermocellum was actively secreted by transformed L. plantarum. In growing L. plantarum cultures, most of the enzymes were irreversibly inactivated when the pH decreased below 4.5. If the transformed strains were to be applied as an inoculum in silage, this pH inactivation might be useful in preventing overdigestion of the crop fibre.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00172547
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  • 4
    Electronic Resource
    Electronic Resource
    Specific quantification of trichoderma reesei cellulases in reconstituted mixtures and its application to cellulase-cellulose binding studies (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 44 (1994), S. 961-966 
    Details
    ISSN: 0006-3592
    Keywords: cellobiohydrolase ; endoglucanase ; adsorption ; hydrolytic efficiency ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Specific quantifications of the major cellulolytic components of the Trichoderma reesei enzyme complex, i.e., endoglucanases I and III and cellobiohydrolases I and II, are described and, employing a defined mixture of these four cellulases reconstituted according to the composition of the native Trichoderma cellulase complex, used to determine the binding of each individual component onto filter paper. During substrate degradation by this enzyme mixture, the specific adsorption of each individual cellulase gradually increases and no preferential binding of one enzyme component in any particular phase of cellulose hydrolysis is found. T. reesei cellobiohydrolases I and II admixed with endoglucanases I and III represent a “full-value” cellulase system that is capable of degrading semicrystalline cellulose efficiently. In comparison with the crude Trichoderma enzyme complex, almost identical adsorption properties and similar hydrolytic efficiency are found for the reconstituted mixture. © 1994 John Wiley & Sons, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260440812
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