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  • 1
    Electronic Resource
    Electronic Resource
    Alkaline cellulases from alkaliphilic Bacillus: Enzymatic properties, genetics, and application to detergents (1997)
    Springer
    Extremophiles 1 (1997), S. 61-66 
    Details
    ISSN: 1433-4909
    Keywords: Key words Alkaliphile ; Bacillus ; Cellulase ; Cloning ; Amino acid sequence ; Detergent
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have isolated a number of alkaliphilic Bacillus that produce alkaline exoenzymes and found a possible use for alkaline cellulase (carboxymethylcellulase) as an additive for improving the cleaning effect of detergents. Enzymatic properties of some candidate cellulases fulfilled the essential requirements for enzymes to be used practically in laundry detergents. Here I describe the properties and possible catalytic mechanism of the hydrolytic reaction and the gene for the industrial alkaline cellulase produced by one of the isolates, Bacillus sp. KSM-635.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007920050015
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Purification and properties of mangano-superoxide dismutase from a strain of alkaliphilic Bacillus (1997)
    Springer
    Extremophiles 1 (1997), S. 74-78 
    Details
    ISSN: 1433-4909
    Keywords: Key words Superoxide dismutase ; Purification ; Alkaliphile ; Bacillus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A mangano-superoxide dismutase (EC 1.15.1.1) was purified to homogeneity from a strain of alkaliphilic Bacillus for the first time. The purified protein, with an isoelectric point of pH 4.5, had a molecular mass of approximately 50 kDa and consisted of two identical subunits (25 kDa). The N-terminal amino acid sequence was Ala-Tyr-Lys-Leu-Pro-Glu-Leu-Pro-Tyr-Ala-Ala-Asn-Ala-Leu-Glu-Pro-His-Ile-Asp-Glu-Ala. The optimum pH and temperature for the reaction were 7.5 and 35°C, respectively. The properties of the superoxide dismutase were compared with those of the enzyme from thermophilic Bacillus stearothermophilus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007920050017
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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