Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.10.3.2 (laccase)
 4,656 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The ability of stationary and shaken Lentinus tigrinus CBS 577.79 liquid cultures to degrade a mixture of polycyclic aromatic hydrocarbons (PAHs) in N-rich (i.e., malt extract glucose, MEG) and in N-limited (low-N Kirk's medium, LNKM) media was investigated. Best results were obtained in shaken cultures where PAHs were degraded by 91% and 97% in MEG and LNKM, respectively; in stationary cultures, on the contrary, the degradation was never higher than 50%. Laccase activity was predominant on MEG while Mn-peroxidase (MnP) was preferentially produced in LNKM. The identification of degradation products showed the presence of several PAH derivatives, such as quinones, dicarboxylated and ring fission derivatives, presumably derived from the action of lignin-modifying enzymes. The presence of some degradation products (e.g., hydroxylated derivatives of anthrone and phenanthrene 9,10-dihydrodiol) suggested the possible involvement of cytochrome P-450-epoxide hydrolase system, the active form of which was found in 7-day-old cultures on MEG. In vitro experiments showed that the MnP from L. tigrinus had wider PAH substrate range and higher oxidation ability than the laccase produced by the same strain.
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PMID:In vivo and in vitro polycyclic aromatic hydrocarbons degradation by Lentinus (Panus) tigrinus CBS 577.79. 2005 9