Solubilization of low-rank coal by Trichoderma atroviride: evidence for the involvement of hydrolytic and oxidative enzymes by using 14C-labelled lignite.
The deuteromycete Trichoderma atroviride is able to solubilize lignite in dependence on a given carbon source for growth. When cultivated on media containing glutamate, this mold excreted a set of different enzymes with hydrolytic activity. Addition of lignite to the growth media induced the synthesis of extracellular lignite-specific esterase activity but no evidence has been provided for its direct involvement in the process of lignite solubilization. Hence, the basic capability of T. atroviride enzymes to degrade a variety of ester and ether bonds at the surface or within the bulky lignite structure was tested using coal following its direct labelling with 14C-alkyl iodide. The participation of hydrolytic and oxidative enzymes in lignite degradation was assessed by measuring the release of 14C radioactivity from selectively alkylated carboxylic and phenolic OH groups. T. atroviride cleaved both carboxylic esters using esterases and the phenolic ether bonds by using oxidative enzymes, most likely laccases.
Hölker
U
U
Botanisches Institut der Universität Bonn, Kirschallee 1, 53115 Bonn, Germany.
Schmiers
H
H
Grosse
S
S
Winkelhöfer
M
M
Polsakiewicz
M
M
Ludwig
S
S
Dohse
J
J
Höfer
M
M
D002250:Carbon Radioisotopes; D003031:Coal / Q000382:microbiology*; D004950:Esterases / Q000378:metabolism*; D042845:Laccase; D010088:Oxidoreductases / Q000378:metabolism*; D012995:Solubility; D017550:Spectroscopy, Fourier Transform Infrared; D014242:Trichoderma / Q000201:enzymology*
D002250:Carbon Radioisotopes; D003031:Coal; D010088:Oxidoreductases; D042845:Laccase; D004950:Esterases