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
URL:
http://dx.doi.org/10.1007/BF00406669
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