Direct rate assessment of laccase catalysed radical formation in lignin by electron paramagnetic resonance spectroscopy

Publikation: Bidrag til tidsskriftTidsskriftartikelfagfællebedømt

Standard

Direct rate assessment of laccase catalysed radical formation in lignin by electron paramagnetic resonance spectroscopy. / Munk, Line; Andersen, Mogens Larsen; Meyer, Anne S.

I: Enzyme and Microbial Technology, Bind 106, 2017, s. 88-96.

Publikation: Bidrag til tidsskriftTidsskriftartikelfagfællebedømt

Harvard

Munk, L, Andersen, ML & Meyer, AS 2017, 'Direct rate assessment of laccase catalysed radical formation in lignin by electron paramagnetic resonance spectroscopy', Enzyme and Microbial Technology, bind 106, s. 88-96. https://doi.org/10.1016/j.enzmictec.2017.07.006

APA

Munk, L., Andersen, M. L., & Meyer, A. S. (2017). Direct rate assessment of laccase catalysed radical formation in lignin by electron paramagnetic resonance spectroscopy. Enzyme and Microbial Technology, 106, 88-96. https://doi.org/10.1016/j.enzmictec.2017.07.006

Vancouver

Munk L, Andersen ML, Meyer AS. Direct rate assessment of laccase catalysed radical formation in lignin by electron paramagnetic resonance spectroscopy. Enzyme and Microbial Technology. 2017;106:88-96. https://doi.org/10.1016/j.enzmictec.2017.07.006

Author

Munk, Line ; Andersen, Mogens Larsen ; Meyer, Anne S. / Direct rate assessment of laccase catalysed radical formation in lignin by electron paramagnetic resonance spectroscopy. I: Enzyme and Microbial Technology. 2017 ; Bind 106. s. 88-96.

Bibtex

@article{6d7956ed94004a32bb90309167b47bbb,
title = "Direct rate assessment of laccase catalysed radical formation in lignin by electron paramagnetic resonance spectroscopy",
abstract = "Laccases (EC 1.10.3.2) catalyse removal of an electron and a proton from phenolic hydroxyl groups, including phenolic hydroxyls in lignins, to form phenoxy radicals during reduction of O2. We employed electron paramagnetic resonance spectroscopy (EPR) for real time measurement of such catalytic radical formation activity on three types of lignin (two types of organosolv lignin, and a lignin rich residue from wheat straw hydrolysis) brought about by two different fungal laccases, derived from Trametes versicolor (Tv) and Myceliophthora thermophila (Mt), respectively. Laccase addition to suspensions of the individual lignin samples produced immediate time and enzyme dose dependent increases in intensity in the EPR signal with g-values in the range 2.0047–2.0050 allowing a direct quantitative monitoring of the radical formation and thus allowed laccase enzyme kinetics assessment on lignin. The experimental data verified that the laccases acted upon the insoluble lignin substrates in the suspensions. When the action on the lignin substrates of the two laccases were compared on equal enzyme dosage levels (by activity units on syringaldazine) the Mt laccase exerted a significantly faster radical formation than the Tv laccase on all three types of lignin substrates. When comparing the equal laccase dose rates on the three lignin substrates the enzymatic radical formation rate on the wheat straw lignin residue was consistently higher than those of the organosolv lignins. The pH-temperature optimum for the radical formation rate in organosolv lignin was determined by response surface methodology to pH 4.8, 33 °C and pH 5.8, 33 °C for the Tv laccase and the Mt laccase, respectively. The results verify direct radical formation action of fungal laccases on lignin without addition of mediators and the EPR methodology provides a new type of enzyme assay of laccases on lignin.",
keywords = "Dose-response treatment, EPR, Laccase kinetics, Phenoxy radicals in lignin, Real time assay",
author = "Line Munk and Andersen, {Mogens Larsen} and Meyer, {Anne S.}",
year = "2017",
doi = "10.1016/j.enzmictec.2017.07.006",
language = "English",
volume = "106",
pages = "88--96",
journal = "Enzyme and Microbial Technology",
issn = "0141-0229",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Direct rate assessment of laccase catalysed radical formation in lignin by electron paramagnetic resonance spectroscopy

AU - Munk, Line

AU - Andersen, Mogens Larsen

AU - Meyer, Anne S.

PY - 2017

Y1 - 2017

N2 - Laccases (EC 1.10.3.2) catalyse removal of an electron and a proton from phenolic hydroxyl groups, including phenolic hydroxyls in lignins, to form phenoxy radicals during reduction of O2. We employed electron paramagnetic resonance spectroscopy (EPR) for real time measurement of such catalytic radical formation activity on three types of lignin (two types of organosolv lignin, and a lignin rich residue from wheat straw hydrolysis) brought about by two different fungal laccases, derived from Trametes versicolor (Tv) and Myceliophthora thermophila (Mt), respectively. Laccase addition to suspensions of the individual lignin samples produced immediate time and enzyme dose dependent increases in intensity in the EPR signal with g-values in the range 2.0047–2.0050 allowing a direct quantitative monitoring of the radical formation and thus allowed laccase enzyme kinetics assessment on lignin. The experimental data verified that the laccases acted upon the insoluble lignin substrates in the suspensions. When the action on the lignin substrates of the two laccases were compared on equal enzyme dosage levels (by activity units on syringaldazine) the Mt laccase exerted a significantly faster radical formation than the Tv laccase on all three types of lignin substrates. When comparing the equal laccase dose rates on the three lignin substrates the enzymatic radical formation rate on the wheat straw lignin residue was consistently higher than those of the organosolv lignins. The pH-temperature optimum for the radical formation rate in organosolv lignin was determined by response surface methodology to pH 4.8, 33 °C and pH 5.8, 33 °C for the Tv laccase and the Mt laccase, respectively. The results verify direct radical formation action of fungal laccases on lignin without addition of mediators and the EPR methodology provides a new type of enzyme assay of laccases on lignin.

AB - Laccases (EC 1.10.3.2) catalyse removal of an electron and a proton from phenolic hydroxyl groups, including phenolic hydroxyls in lignins, to form phenoxy radicals during reduction of O2. We employed electron paramagnetic resonance spectroscopy (EPR) for real time measurement of such catalytic radical formation activity on three types of lignin (two types of organosolv lignin, and a lignin rich residue from wheat straw hydrolysis) brought about by two different fungal laccases, derived from Trametes versicolor (Tv) and Myceliophthora thermophila (Mt), respectively. Laccase addition to suspensions of the individual lignin samples produced immediate time and enzyme dose dependent increases in intensity in the EPR signal with g-values in the range 2.0047–2.0050 allowing a direct quantitative monitoring of the radical formation and thus allowed laccase enzyme kinetics assessment on lignin. The experimental data verified that the laccases acted upon the insoluble lignin substrates in the suspensions. When the action on the lignin substrates of the two laccases were compared on equal enzyme dosage levels (by activity units on syringaldazine) the Mt laccase exerted a significantly faster radical formation than the Tv laccase on all three types of lignin substrates. When comparing the equal laccase dose rates on the three lignin substrates the enzymatic radical formation rate on the wheat straw lignin residue was consistently higher than those of the organosolv lignins. The pH-temperature optimum for the radical formation rate in organosolv lignin was determined by response surface methodology to pH 4.8, 33 °C and pH 5.8, 33 °C for the Tv laccase and the Mt laccase, respectively. The results verify direct radical formation action of fungal laccases on lignin without addition of mediators and the EPR methodology provides a new type of enzyme assay of laccases on lignin.

KW - Dose-response treatment

KW - EPR

KW - Laccase kinetics

KW - Phenoxy radicals in lignin

KW - Real time assay

U2 - 10.1016/j.enzmictec.2017.07.006

DO - 10.1016/j.enzmictec.2017.07.006

M3 - Journal article

C2 - 28859815

AN - SCOPUS:85025456536

VL - 106

SP - 88

EP - 96

JO - Enzyme and Microbial Technology

JF - Enzyme and Microbial Technology

SN - 0141-0229

ER -

ID: 196166975