Abstract
Multicopper oxidases (MCO) catalyze the biological oxidation of various aromatic substrates and have been identified in plants, insects, bacteria, and wood rotting fungi. In nature, they are involved in biodegradation of biopolymers such as lignin and humic compounds, but have also been tested for various industrial applications. In fungi, MCOs have been shown to play important roles during their life cycles, such as in fruiting body formation, pigment formation and pathogenicity. Coprophilous fungi, which grow on the dung of herbivores, appear to encode an unexpectedly high number of enzymes capable of at least partly degrading lignin. This study compared the MCO-coding capacity of the coprophilous filamentous ascomycetes Podospora anserina and Sordaria macrospora with closely related non-coprophilous members of the order Sordariales. An increase of MCO genes in coprophilic members of the Sordariales most probably occurred by gene duplication and horizontal gene transfer events.
Highlights
Multicopper oxidases (MCOs) are a family of enzymes that contain copper atoms in their catalytic center, and are capable of coupling the oxidation of a substrate, e.g. polyphenols, aromatic amines and a variety of other components, with a four-electron reduction of molecular oxygen to water [1]
A total of 49 MCO amino acid sequences were obtained from the genomic databases of N. crassa, S. macrospora, P. anserina and C. globosum, including putative laccases, ascorbate oxidases, bilirubin oxidases and ferroxidases (Table 1)
In the four fungi analyzed, most of the identified MCOs belong to the laccase group
Summary
Multicopper oxidases (MCOs) are a family of enzymes that contain copper atoms in their catalytic center, and are capable of coupling the oxidation of a substrate, e.g. polyphenols, aromatic amines and a variety of other components, with a four-electron reduction of molecular oxygen to water [1]. While plant laccases mainly participate in lignin polymer formation, fungal laccases are involved in the degradation of lignin and humic acids, and have important roles in developmental processes such as fruiting body development and pigmentation. Because they oxidize, polymerize, or transform phenolic or anthropogenic compounds into less toxic derivatives, fungal laccases have been used for various biotechnological applications such as food processing, bioremediation of waste water, and removal of lignin from wood fibers [4,5,6,7].
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