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  • 1
    Electronic Resource
    Electronic Resource
    Alkaline detergent enzymes from alkaliphiles: enzymatic properties, genetics, and structures (1998)
    Springer
    Extremophiles 2 (1998), S. 185-190 
    Details
    ISSN: 1433-4909
    Keywords: Key words Alkaliphile ; Bacillus ; Detergent enzyme ; α-Amylase ; Debranching enzyme ; Protease ; Cellulase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The cleaning power of detergents seems to have peaked; all detergents contain similar ingredients and are based on similar detergency mechanisms. To improve detergency, modern types of heavy-duty powder detegents and automatic dishwasher detergents usually contain one or more enzymes, such as protease, amylase, cellulase, and lipase. Alkaliphilic Bacillus strains are often good sources of alkaline extracellular enzymes, the properties of which fulfil the essential requirements for enzymes to be used in detergents. We have isolated numbers of alkaliphilic Bacillus that produce such alkaline detergent enzymes, including cellulase (CMCase), protease, α-amylase, and debranching enzymes, and have succeeded in large-scale industrial production of some of these enzymes. Here, we describe the enzymatic properties, genetics, and structures of the detergent enzymes that we have developed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007920050059
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  • 2
    Electronic Resource
    Electronic Resource
    Highly alkaline pectate lyase Pel-4A from alkaliphilic Bacillus sp. strain P-4-N: its catalytic properties and deduced amino acid sequence (2000)
    Springer
    Extremophiles 4 (2000), S. 377-383 
    Details
    ISSN: 1433-4909
    Keywords: Key words Alkaliphile ; Pectate lyase ; Cloning ; Bacillus ; Salt dependency
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The gene for a highly alkaline pectate lyase, Pel-4A, from alkaliphilic Bacillus sp. strain P-4-N was cloned, sequenced, and overexpressed in Bacillus subtilis cells. The deduced amino acid sequence of the mature enzyme (318 amino acids, 34 805 Da) showed moderate homology to those of known pectate lyases in the polysaccharide lyase family 1. The purified recombinant enzyme had an isoelectric point of pH 9.7 and a molecular mass of 34 kDa, and exhibited a very high specific activity compared with known pectate lyases reported so far. The enzyme activity was stimulated 1.6 fold by addition of NaCl at an optimum of 100 mM. When Pel-4A was stored at 50°C for 60 h, striking stabilization by 100 mM NaCl was observed in a pH range from 5 to 11.5, whereas it was stable only around pH 11 in the absence of NaCl.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007920070008
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    Paper (German National Licenses)
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