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  • 1
    Electronic Resource
    Electronic Resource
    Properties of extremely thermostable proteases from anaerobic hyperthermophilic bacteria (1991)
    Springer
    Applied microbiology and biotechnology 34 (1991), S. 715-719 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Hyperthermostable proteases were characterized from five archaeobacterial species (Thermococcus celer, T. stetteri, Thermococcus strain AN 1, T. litoralis, Staphylothermus marinus) and the hyperthermophilic eubacterium Thermobacteroides proteolyticus. These proteases, which were found to be of the serine type, exhibited a preference for phenylalanine in the carboxylic side of the peptide. The enzymes from Thermococcus stetteri and T. litoralis hydrolysed most substrates (peptides) tested. All proteases were extremely thermostable and demonstrated optimal activities between 80 and 95°C. The pH optimum was either neutral (T. celer, Thermococcus strain AN 1) or alkaline. The protease of Thermobacteroides proteolyticus was optimally active at pH 9.5. Zymogram staining showed the presence of multiple protease bands for all strains investigated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00169339
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Purification and properties of a hyperthermoactive α-amylase from the archaeobacterium Pyrococcus woesei (1991)
    Springer
    Archives of microbiology 155 (1991), S. 572-578 
    Details
    ISSN: 1432-072X
    Keywords: Hyperthermophilic bacteria ; Thermostability ; Alpha-amylase ; Pyrococcus woesei
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The cultivation of the hyperthermophilic archaeobacterium Pyrococcus woesei on starch under continuous gassing (80% H2:20% CO2) caused the formation of 250 U/l of an extremely thermoactive and thermostable α-amylase. In a complex medium without elemental sulphur under 80% N2 and 20% CO2 atmosphere enzyme production could be elevated up to 1000 U/l. Pyrococcus woesei grew preferentially on poly-and oligosaccharides. The amylolytic enzyme formation was constitutive. Enzyme production was also observed in continuous culture at dilution rates from 0.1 to 0.4 h-1. A 20-fold enrichment of α-amylase was achieved after adsorption of the enzyme onto starch and its desorption by preparative gel electrophoresis. The α-amylase consisted of a single subunit with a molecular mass of 70 000 and was catalytically active at a temperature range between 40°C and 130°C. Enzymatic activity was detected even after autoclaving at a pressure of 2 bars at 120°C for 5 h. The purified enzyme hydrolyzed exclusively α-1,4-glycosidic linkages present in glucose polymers of various sizes. Unlike many α-amylases from anaerobes the enzyme from P. woesei was unable to attack short chain oligosaccharides with a chain length between 2 and 6 glucose units.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00245352
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Isolierung eines hitzestabilen Entzweigungsenzyms (Pullulanase) mit industrieller Relevanz aus einem neuen Fervidobacterium (1992)
    Weinheim : Wiley-Blackwell
    Chemie Ingenieur Technik - CIT 64 (1992), S. 548-550 
    Details
    ISSN: 0009-286X
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cite.330640615
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    Paper (German National Licenses)
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