A manganese-peroxidase from Lentinus edodes solid-state cultures was purified and its ability to bring about the oxidation of veratryl alcohol was investigated. Such investigations were carried out in the absence and in the presence of reduced glutathione (GSH), as a thiol-donor. Two different biodegradative pathways were identified, in the former case leading to aromatic ring cleavage, side chain oxidation and dimerization, while in the latter case veratraldehyde was recovered as the only metabolite.
Veratryl alcohol oxidation by manganese-dependent peroxidase from Lentinus edodes
Crestini C;
1996-01-01
Abstract
A manganese-peroxidase from Lentinus edodes solid-state cultures was purified and its ability to bring about the oxidation of veratryl alcohol was investigated. Such investigations were carried out in the absence and in the presence of reduced glutathione (GSH), as a thiol-donor. Two different biodegradative pathways were identified, in the former case leading to aromatic ring cleavage, side chain oxidation and dimerization, while in the latter case veratraldehyde was recovered as the only metabolite.File in questo prodotto:
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