Stabilization of lignin peroxidases in white rot fungi by tryptophan

Patrick J. Collins, James A Field, Pauline Teunissen, Alan D W Dobson

Research output: Contribution to journalArticle

62 Citations (Scopus)

Abstract

Supplementation of various cultures of white rot fungi with tryptophan was found so 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 (US)
Pages (from-to)2543-2548
Number of pages6
JournalApplied and Environmental Microbiology
Volume63
Issue number7
StatePublished - Jul 1997
Externally publishedYes

Fingerprint

lignin peroxidase
white-rot fungi
Tryptophan
tryptophan
lignin
stabilization
Fungi
fungus
alcohol
Azo Compounds
alcohols
azo dyes
Recycling
indoles
enzyme
recycling
dye
Enzymes
enzymes
oxidation

ASJC Scopus subject areas

  • Environmental Science(all)
  • Biotechnology
  • Microbiology

Cite this

Collins, P. J., Field, J. A., Teunissen, P., & Dobson, A. D. W. (1997). Stabilization of lignin peroxidases in white rot fungi by tryptophan. Applied and Environmental Microbiology, 63(7), 2543-2548.

Stabilization of lignin peroxidases in white rot fungi by tryptophan. / Collins, Patrick J.; Field, James A; Teunissen, Pauline; Dobson, Alan D W.

In: Applied and Environmental Microbiology, Vol. 63, No. 7, 07.1997, p. 2543-2548.

Research output: Contribution to journalArticle

Collins, PJ, Field, JA, Teunissen, P & Dobson, ADW 1997, 'Stabilization of lignin peroxidases in white rot fungi by tryptophan', Applied and Environmental Microbiology, vol. 63, no. 7, pp. 2543-2548.
Collins, Patrick J. ; Field, James A ; Teunissen, Pauline ; Dobson, Alan D W. / Stabilization of lignin peroxidases in white rot fungi by tryptophan. In: Applied and Environmental Microbiology. 1997 ; Vol. 63, No. 7. pp. 2543-2548.
@article{a984f55838a340e09ba6e671fcf519ef,
title = "Stabilization of lignin peroxidases in white rot fungi by tryptophan",
abstract = "Supplementation of various cultures of white rot fungi with tryptophan was found so 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.",
author = "Collins, {Patrick J.} and Field, {James A} and Pauline Teunissen and Dobson, {Alan D W}",
year = "1997",
month = "7",
language = "English (US)",
volume = "63",
pages = "2543--2548",
journal = "Applied and Environmental Microbiology",
issn = "0099-2240",
publisher = "American Society for Microbiology",
number = "7",

}

TY - JOUR

T1 - Stabilization of lignin peroxidases in white rot fungi by tryptophan

AU - Collins, Patrick J.

AU - Field, James A

AU - Teunissen, Pauline

AU - Dobson, Alan D W

PY - 1997/7

Y1 - 1997/7

N2 - Supplementation of various cultures of white rot fungi with tryptophan was found so 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.

AB - Supplementation of various cultures of white rot fungi with tryptophan was found so 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.

UR - http://www.scopus.com/inward/record.url?scp=0030796654&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030796654&partnerID=8YFLogxK

M3 - Article

VL - 63

SP - 2543

EP - 2548

JO - Applied and Environmental Microbiology

JF - Applied and Environmental Microbiology

SN - 0099-2240

IS - 7

ER -