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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 123 (1979), S. 319-321 
    ISSN: 1432-072X
    Keywords: Basidiomycete ; Vanillic acid ; Vanillate hydroxylase ; Monooxygenase ; Methoxy-p-hydroquinone ; Lignin biodegradation ; Phanerochaete chrysosporium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A soluble enzyme fraction from Phanerochaete chrysosporium catalyzed the oxidative decarboxylation of vanillic acid to methoxy-p-hydroquinone. The enzyme, partially purified by ammonium sulfate precipitation, required NADPH and molecular oxygen for activity. NADH was not effective. Optimal activity was displayed between pH 7.5–8.5. Neither EDTA, KCN, NaN3, nor o-phenanthroline (5 mM) were inhibitory. The enzyme was inducible with maximal activity displayed after incubation of previously grown cells with 0.1% vanillate for 30h.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 121 (1979), S. 37-41 
    ISSN: 1432-072X
    Keywords: Basidiomycete ; Basidiospores ; Fruit body ; Hymenium ; Catabolite repression ; Nitrogen repression ; cAMP ; Phanerochaete chrysosporium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In Phanerochaete chrysosporium fruit body formations is subject to strong catabolite repression by glucose in the presence of physiological levels of nitrogen. Walseth cellulose was found to be the best source of carbon for the induction of fruit body and consequent basidiospore synthesis. Ejected basidiospores collected from cultures grown under these conditions for two weeks are contaminated with neither conidia nor mycelial fragments and are therefore suitable for genetic analysis of recombination. Under conditions of nitrogen limitation, the glucose catabolite repression of fruit body synthesis was relieved. Exogenous adenosine 3′,5′-monophosphate but not other related nucleotides, also relieved glucose catabolite repression of fruit body formation.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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