Different fungal manganese-oxidizing peroxidases: a comparison between Bjerkandera sp. and Phanerochaete chrysosporium

Molecular characterisation of a versatile peroxidase from a Bjerkandera strain

“…A novel class of ligninolytic peroxidases, named versatile peroxidases, with high affinity for manganese and dyes, has been described; these enzymes can also oxidise 2,6-dimethoxyphenol (DMP) and veratryl alcohol (VA) in a manganese-independent reaction (Camarero et al, 1996(Camarero et al, , 1999(Camarero et al, , 2000Giardina et al, 2000;Heinfling et al, 1998a,b,c;Martinez, 2002;Mester and Field, 1998;Palma et al, 2000;Ruiz-Duenas et al, 1999b. Until now, however, those enzymes have only been isolated from Pleurotus ostreatus, Pleurotus eryngii, Pleurotus pulmonarius, Bjerkandera adusta and Bjerkandera sp.…”

Laccase-Catalyzed Oxidation of Mn 2+ in the Presence of Natural Mn 3+ Chelators as a Novel Source of Extracellular H 2 O 2 Production and Its Impact on Manganese Peroxidase

“…This is facilitated by fungal organic acids such as oxalate or malonate upon chelation of the highly reactive Mn 3ϩ state (4, 20-22, 40, 43). MnP catalyzes the oxidation of lignin, humic substances, and many organopollutants (16,20,29). Extracellular H 2 O 2 is required as a substrate for ligninolytic peroxidases.…”

A practical culture technique for enhanced production of manganese peroxidase by Anthracophyllum discolor Sp4

“…The K M values for Bjerkandera sp. obtained using the H 2 O 2 showed a variation of between 3 and 5 µM (Palma et al, 2000) which could be considered lower as compared with the MnP from A. discolor Sp4. The optimum pH range was between 4.5 and 5.5, with the relative activity dropping by 20% at pH 6.5 and being inactivated at pH 9.0 (data not shown).…”

“…The apparent K M values of the purified MnP for 2,6-DMP and H 2 O 2 were 25 µM and 37 µM, respectively, indicating high affinity for both the substrates. Previous studies on kinetic parameters from Phanerochaete chrysosporium using 2,6-DMP as substrate have shown that K M values ranged from 7 to 29 µM (Palma et al, 2000;Ürek and Pazarlioğlu, 2004) depending on the operational conditions and the isoenzymes produced. They were comparable and in the same magnitude order Phanerochaete chrysosporium ranged from 5 to 71 µM (Palma et al, 2000;Ürek and Pazarlioğlu, 2004) and were comparable to the results obtained for MnP from A. discolor Sp4.…”