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  • Cu‐ZSM‐5  (1)
  • Termitomyces clypeatus  (1)
  • Springer  (2)
  • 2015-2019
  • 1995-1999  (2)
  • 1935-1939
  • 1999  (1)
  • 1995  (1)
  • 1939
Collection
Publisher
  • Springer  (2)
Years
  • 2015-2019
  • 1995-1999  (2)
  • 1935-1939
Year
  • 1999  (1)
  • 1995  (1)
  • 1939
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Catalysis letters 61 (1999), S. 179-186 
    ISSN: 1572-879X
    Keywords: CO oxidation ; Cu‐ZSM‐5 ; zeolites ; DFT
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The catalytic oxidation of CO by Cu‐exchanged high‐silica zeolites (e.g., ZSM‐5) has been investigated theoretically using density functional theory. Calculations reveal two distinct, parallel pathways for oxidation of CO: (i) adsorption of O2= on a reduced Cu site followed by O atom abstraction by CO, and (ii) adsorption of CO followed by its reaction with O2= to form a cyclic compound which decomposes to form CO2=. The reduced site is regenerated via two different pathways, both of which involve oxidation of one or more CO molecules: (i) abstraction of atomic oxygen by CO from the oxidized active site, and (ii) formation of a carbonate species followed by its reaction with a molecule of CO. The relevance of these reactions to the reduction of NO is discussed.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    World journal of microbiology and biotechnology 11 (1995), S. 359-360 
    ISSN: 1573-0972
    Keywords: α-L-Arabino furanosidase ; Termitomyces clypeatus ; xylanase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Termitomyces clypeatus produced xylanase and α-L-arabinofuranosidase simultaneously in various media. The arabinofuranosidase had pH and temperature optima of 5.5 and 50°C, respectively, and was stable at 50°C for 30 min and at pH values from 2 to 5. The partially purified enzyme was distinct from xylanase present in the same medium.
    Type of Medium: Electronic Resource
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