Previous Article | Next Article ![]()
Appl. Environ. Microbiol., May 1995, 1876-1880, Vol 61, No. 5
R Bourbonnais, MG Paice, ID Reid, P Lanthier and M Yaguchi
Two laccase isozymes (I and II) produced by the white-rot fungus Trametes
versicolor were purified, and their reactivities towards various substrates
and lignins were studied. The N-terminal amino acid sequences of these
enzymes were determined and compared to other known laccase sequences.
Laccase II showed a very high sequence similarity to a laccase which was
previously reported to depolymerize lignin. The reactivities of the two
isozymes on most of the substrates tested were similar, but there were some
differences in the oxidation rate of polymeric substrates. We found that
the two laccases produced similar qualitative effects on kraft lignin and
residual lignin in kraft pulp, with no evidence of a marked preference for
depolymerization by either enzyme. However, the presence of the mediator
2,2'-azinobis(3- ethylbenzthiazoline-6-sulfonate) prevented and reversed
the polymerization of kraft lignin by either laccase. The delignification
of hardwood and softwood kraft pulps with the two isozymes and the mediator
was compared; either laccase was able to reduce the kappa number of pulp,
but only in the presence of 2,2'-azinobis(3-
ethylbenzthiazoline-6-sulfonate).
Copyright © 1995, American Society for Microbiology
Lignin oxidation by laccase isozymes from Trametes versicolor and role of the mediator 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) in kraft lignin depolymerization
Pulp and Paper Research Institute of Canada, Pointe Claire, Quebec, Ontario.
This article has been cited by other articles:
| J. Bacteriol. | Microbiol. Mol. Biol. Rev. | Eukaryot. Cell | All ASM Journals |
|---|