Manganese peroxidase (Mn peroxidase) catalyses the oxidation of Mn(II) to Mn(III), a diffusible non-specific oxidant likely to be involved in the transformation of polyphenolic macromolecules from brown coal by the white-rot fungus Phanerochaete chrysosporium. We report here that solubilised macromolecules from Morwell brown coal were depolymerised by Mn(III) ions when incubated under hyperbaric O2 However, under N2 or air they were polymerised, suggesting that net depolymerisation by Mn(III) requires molecular oxygen to inhibit coupling of coal radicals. Coal macromolecules were also polymerised when separated by a semipermeable membrane from a culture of P. chrysosporium or from a solution of Mn peroxidase, Mn(II) and H2O2, probably by Mn(III) crossing the membrane. In oxygenated cultures in which Mn peroxidase was up-regulated by Mn(II), the extent of depolymerisation correlated with cumulative Mn peroxidase activity suggesting that Mn-peroxidase-generated Mn(III) has a central role in initial depolymerisation of coal molecules in vivo. However, mutant ME446-B17-1, which produces Mn peroxidase but not lignin peroxidase, polymerised coal macromolecules in oxygenated cultures. In sum, it appears Mn peroxidase can both polymerise,and depolymerise brown coal macromolecules and that, in vivo, both hyperbaric O2 and lignin peroxidase are also required to force net depolymerisation to products assimilable by cells.
|Number of pages||7|
|Journal||Applied Microbiology and Biotechnology|
|Publication status||Published - Jun 1998|
Bibliographical noteFunding Information:
Acknowledgements We are grateful to Shree Dhawale for peroxidase-negative mutants of P. chrysosporium. This work was funded by grants from the Australian Research Council and Flinders University.