Transformation of macromolecules from a brown coal by lignin peroxidase |
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Authors: | J P Ralph D E A Catcheside |
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Institution: | (1) School of Biological Sciences, Flinders University of South Australia, Bedford Park, SA 5042, Australia e-mail: David.Catcheside@flinders.edu.au Tel.: +618-8201-2335 Fax: +618-8201-3015, AU |
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Abstract: | Indirect evidence has suggested that lignin peroxidase (LiP) of the white-rot fungus Phanerochaete chrysosporium catalyses oxidative decolourisation and depolymerisation of macromolecules from brown coal in vivo. In this study we show
that LiP catalyses these transformations in vitro. Unmethylated (USC45 coal) and methylated (MWSC6 coal) fractions of solubilised
macromolecules (M
r > 30 000) from a brown coal were treated with a semi-purified preparation of LiP isozymes from P. chrysosporium. Both coal fractions were decolourised, losing between 26% and 39% of their absorbance at both 280 nm and 400 nm, in reactions
that had an absolute requirement for H2O2 and veratryl alcohol. Neither coal fraction was transformed when the enzyme was heat-inactivated or in the presence of the
LiP inhibitor metavanadate. Gel-permeation chromatography showed that MWSC6 coal but not USC45 was depolymerised and yielded
low-molecular-mass (M
r < 30 000) fragments. Nine monomeric products were identified by GC-MS.
Received: 20 March 1998 / Received revision: 3 September 1998 / Accepted: 3 September 1998 |
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