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  • Salt dependency  (1)
  • europium  (1)
  • 2000-2004  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of sol gel science and technology 19 (2000), S. 357-360 
    ISSN: 1573-4846
    Keywords: photoreduction ; europium ; inorganic-organic hybrid material ; ligand
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Eu2+-doped inorganic-organic hybrid materials, which are potentially suitable for a tunable laser in the near ultra violet and blue region, were prepared through the photoreduction of Eu3+ ions in the materials under the irradiation of the fourth harmonic wave light (266 nm) of the Nd:YAG laser. The hybrid materials doped with Eu3+ ions were prepared from Si(OCH3)4, CH3Si(OCH3)3, EuCl3 and chloropropyltrimethoxysilane (CPTM). After the prehydrolized silica sol was added to the Eu3+-containing solution, Eu3+-doped transparent inorganic-organic hybrid material was obtained by drying at 50°C. The emission peak around 450–475 nm due to the charge transfer transition (5d-4f) of Eu2+ ions increased with the laser irradiation time. Eu3+ ions were effectively photoreduced to Eu2+ ions in pore-free materials prepared at high CPTM to Eu3+ ratios. Eu2+ ions were generated by the photodecomposition of the bond between Eu3+ and Cl (Cl− or Cl(CH2)3 in CPTM).
    Type of Medium: Electronic Resource
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  • 2
    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
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