Stabilization of lignin peroxidases in white rot fungi by tryptophan.

P.J. Collins, J.A. Field, P. Teunissen, A.D.W. Dobson

Research output: Contribution to journalArticleAcademicpeer-review

80 Citations (Scopus)

Abstract

Supplementation of various cultures of white rot fungi with tryptophan was found to have a large stimulatory effect on lignin peroxidase activity levels. This enhancement was greater than that observed in the presence of the lignin peroxidase recycling agent veratryl alcohol. Using reverse transcription-PCR, we found that tryptophan does not act to induce lignin peroxidase expression at the level of gene transcription. Instead, the activity enhancement observed is likely to result from the protective effect of tryptophan against H2O2 inactivation. In experiments using a partially purified lignin peroxidase preparation, tryptophan and its derivative indole were determined to function in the same way as veratryl alcohol in converting compound II, an oxidized form of lignin peroxidase, to ferric enzyme, thereby completing the catalytic cycle. Furthermore, tryptophan was found to be a better substrate for lignin peroxidase than veratryl alcohol. Inclusion of either tryptophan or indole enhanced the oxidation of the azo dyes methyl orange and Eriochrome blue black. Stimulation of azo dye oxidations by veratryl alcohol has previously been shown to be due to its enzyme recycling function. Our data allow us to propose that tryptophan stabilizes lignin peroxidase by acting as a reductant for the enzyme.
Original languageEnglish
Pages (from-to)2543-2548
JournalApplied and Environmental Microbiology
Volume63
Issue number7
Publication statusPublished - 1997

Fingerprint

Dive into the research topics of 'Stabilization of lignin peroxidases in white rot fungi by tryptophan.'. Together they form a unique fingerprint.

Cite this