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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Bulletin of environmental contamination and toxicology 59 (1997), S. 238-245 
    ISSN: 1432-0800
    Source: Springer Online Journal Archives 1860-2000
    Topics: Energy, Environment Protection, Nuclear Power Engineering , Medicine
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 21 (1998), S. 292-295 
    ISSN: 1476-5535
    Keywords: Keywords: castor oil; hydrolysis; lipase; metal ions; Pseudomonas aeruginosa
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The ability of an extracellular lipase from Pseudomonas aeruginosa KKA-5 to commence hydrolysis of castor oil in the presence of various metal chlorides, was investigated. Apart from CaCl2 (commonly used for castor oil hydrolysis), AlCl3 (group IIIB), CrCl3 (group VIA) and MgCl2 (group IIA) displayed enhanced hydrolysis capability. Specifically, our statistics show that with respect to time, when Cr3+ was used, hydrolysis of castor oil was four times faster than that of calcium, and 1.6 times faster with regards to Al3+. The chlorides of group VIII and alkali metals had no effect on hydrolysis. Group IV metal chlorides did not enhance lipase activity and inhibited castor oil hydrolysis. The effect of metal ions from other groups on lipase activity is also reported.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 20 (1998), S. 304-307 
    ISSN: 1476-5535
    Keywords: Keywords: calcium; castor oil; hydrolysis; lipase; Pseudomonas aeruginosa; purification
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: An extracellular lipase (triacylglycerol acylhydrolase, EC 3.1.1.3) from Pseudomonas aeruginosa KKA-5 hydrolyzed castor oil by 90%. Purification of this castor oil-hydrolyzing lipase included ammonium sulfate precipitation and successive hydroxylapatite column chromatography. The enzyme was purified 518-fold. It was homogeneous electrophoretically and its molecular weight was estimated to be 30 kDa. The enzyme was stable up to 45°C and retained its activity in the alkaline pH range. Lipase was highly stable in the presence of aqueous organic solvents like methanol and ethanol. It was weakly inhibited in the presence of acetone. The anionic surfactant, sodium dodecyl sulfate, was inhibitory while the cationic surfactants, Triton X-100 and Tween-80 appreciably enhanced activity. Lipase was stabilized significantly by Ca2+. Inactivation of the enzyme by EDTA was overcome by sequential CaCl2 treatment. This finding suggests the existence of a calcium-binding site in Pseudomonas aeruginosa KKA-5 lipase.
    Type of Medium: Electronic Resource
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