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Regulation of the synthesis of aryl metabolites by phospholipid sources in the white-rot fungus Bjerkandera adusta
Authors:Carmen Lapadatescu  Christian Giniès  Aleth Djian  Henry-Eric Spinnler  Jean-Luc Le Quéré  Pascal Bonnarme
Institution:Laboratoire de Recherches sur les Ar?mes, Institut National de la Recherche Agronomique, 17 rue Sully, F-21034 Dijon Cedex, France, FR
Laboratoire de Génie et Microbiologie des Procédés Alimentaires (LGMPA), CBAI, Institut National de la Recherche Agronomique, F-78850 Thiverval-Grignon, France e-mail: bonnarme@platon.grignon.inra.fr Tel. +331-30815388; Fax +331-30815597, FR
Abstract:The white-rot basidiomycete Bjerkandera adusta was cultivated in a liquid medium enriched with l-phenylalanine and various phospholipid sources (lecithin, egg yolk and asolectin). Three aromatic metabolites (benzaldehyde, benzyl alcohol and benzoic acid) were produced under these culture conditions. High concentrations of benzaldehyde (404 mg l–1) were obtained when the cultures were supplemented with 10 g lecithin l–1. Benzyl alcohol production was promoted when the strain was grown with 5 or 10 g lecithin l–1. In the absence of or with a low concentration of lecithin (2.5 g l–1), benzoic acid was the major aryl metabolite synthesized. The results presented here indicate that aryl alcohol oxidase, an extracellular enzyme catalyzing the oxidation of benzyl alcohol into benzaldehyde, was maximally detected when significant amounts of benzaldehyde were produced. Aryl alcohol oxidase activity was significantly enhanced in the presence of elevated concentrations of phospholipid sources. Together with lignin peroxidase, methoxylated and hydroxylated aryl metabolites were also synthesized under these culture conditions. The possible involvement of phospholipids in the synthesis of aryl metabolites is discussed. Received: 7 August 1998 / Accepted: 30 November 1998
Keywords:Benzaldehyde  Benzyl alcohol  Benzoic acid  Aryl metabolites  Bjerkandera adusta  Phospholipid sources  Fungal metabolism  Aryl alcohol oxidase
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