AbstractTwo oxidation products of veratryl alcohol were isolated from ligninolytic cultures of Phanerochaete chrysosporium. After purification the compounds were characterized by 1H-NMR, mass spectrometry and infrared spectrometry. The structural information suggests that the compounds are two isomers of a ring cleavage product from veratryl alcohol. Both compounds were also found as by-products when veratryl alcohol was oxidized to veratraldehyde with the crude extracellular ligninase preparation
A manganese-peroxidase from Lentinus edodes solid-state cultures was purified and its ability to...
A manganese-peroxidase from Lentinus edodes solid-state cultures was purified and its ability to...
Abstract--The vanous culture conditions for production of lignin peroxidase were examined by use of ...
AbstractTwo oxidation products of veratryl alcohol were isolated from ligninolytic cultures of Phane...
AbstractThe oxidation of veratryl alcohol by the lignin peroxidase of Phanerochaete chrysosporium wa...
AbstractThe oxidative capacity of the ligninase from Phanerochaete chrysosporium toward monomethoxyl...
The degradation pathway of vanillyl and veratryl alcohol by Lentinus edodes extracellular enzymes wa...
The degradation pathway of vanillyl and veratryl alcohol by Lentinus edodes extracellular enzyme...
AbstractEnzymatic oxidation of veratryl alcohol yielded a new ring cleavage product (δ-lactone) in a...
Abstract--Veratryl alcohol was found in ligninolytic culture of Coriolus versicolor. The structure o...
AbstractThe degradation of a β-O-4 lignin substructure model dimer, 4-ethoxy-3-methoxyphenylglycerol...
A manganese-peroxidase from Lentinus edodes solid-state cultures was purified and its ability to bri...
AbstractMethyl oxalate of arylglycerol was formed as an aromatic ring cleavage product in degradatio...
The kinetics of decay of veratryl alcohol radical cation, generated by cerium(IV) ammonium nitrate i...
Benzo(a)pyrene was oxidized with crude and purified extracellular ligninase preparations from Phaner...
A manganese-peroxidase from Lentinus edodes solid-state cultures was purified and its ability to...
A manganese-peroxidase from Lentinus edodes solid-state cultures was purified and its ability to...
Abstract--The vanous culture conditions for production of lignin peroxidase were examined by use of ...
AbstractTwo oxidation products of veratryl alcohol were isolated from ligninolytic cultures of Phane...
AbstractThe oxidation of veratryl alcohol by the lignin peroxidase of Phanerochaete chrysosporium wa...
AbstractThe oxidative capacity of the ligninase from Phanerochaete chrysosporium toward monomethoxyl...
The degradation pathway of vanillyl and veratryl alcohol by Lentinus edodes extracellular enzymes wa...
The degradation pathway of vanillyl and veratryl alcohol by Lentinus edodes extracellular enzyme...
AbstractEnzymatic oxidation of veratryl alcohol yielded a new ring cleavage product (δ-lactone) in a...
Abstract--Veratryl alcohol was found in ligninolytic culture of Coriolus versicolor. The structure o...
AbstractThe degradation of a β-O-4 lignin substructure model dimer, 4-ethoxy-3-methoxyphenylglycerol...
A manganese-peroxidase from Lentinus edodes solid-state cultures was purified and its ability to bri...
AbstractMethyl oxalate of arylglycerol was formed as an aromatic ring cleavage product in degradatio...
The kinetics of decay of veratryl alcohol radical cation, generated by cerium(IV) ammonium nitrate i...
Benzo(a)pyrene was oxidized with crude and purified extracellular ligninase preparations from Phaner...
A manganese-peroxidase from Lentinus edodes solid-state cultures was purified and its ability to...
A manganese-peroxidase from Lentinus edodes solid-state cultures was purified and its ability to...
Abstract--The vanous culture conditions for production of lignin peroxidase were examined by use of ...