Blue laccase from Galerina sp.: Properties and potential for Kraft lignin demethylation

Victor Ibrahim; Laura Mendoza; Gashaw Mamo; Rajni Hatti-Kaul

doi:10.1016/j.procbio.2010.07.013

Blue laccase from Galerina sp.: Properties and potential for Kraft lignin demethylation

Victor Ibrahim, Laura Mendoza, Gashaw Mamo, Rajni Hatti-Kaul

Research output: Contribution to journal › Article › peer-review

Abstract

We purified a laccase isoenzyme, Lad 1 from Galerina sp. HC1 using a combination of anion exchange- and hydrophobic interaction chromatography. Lad l has a molecular mass of 64 kDa, an isoelectric point of 4, and 3.35 copper atoms/enzyme molecule. The enzyme has features typical of fungal blue laccases. The sequences of two internal peptides were highly similar to reported laccase sequences from other fungi such as Trametes sp. Lad 1 exhibited optimal activity on substrate 2,2'-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) at pH 3 and 60 degrees C. It had high stability at <= 20 degrees C and at high pH. Lad 1 exhibited high substrate affinity and the highest catalytic efficiency reported among laccases for ABTS, and among the lowest for syringaldazine. The most potent inhibitors of Lad 1 were sodium azide, sodium cyanide, disulfide reducing agents, and metal ions in the order Li+ > Sn2+ > Hg2+. The laccase efficiently catalyzed demethylation of eucalyptus hard wood Kraft lignin. (C) 2010 Elsevier Ltd. All rights reserved.

Original language	English
Pages (from-to)	379-384
Journal	Process Biochemistry
Volume	46
Issue number	1
DOIs	https://doi.org/10.1016/j.procbio.2010.07.013
Publication status	Published - 2011

Subject classification (UKÄ)

Industrial Biotechnology

Free keywords

Laccase
Galerina sp.
Oxygen consumption
Inhibition
Lignin
Demethylation

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10.1016/j.procbio.2010.07.013

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title = "Blue laccase from Galerina sp.: Properties and potential for Kraft lignin demethylation",

abstract = "We purified a laccase isoenzyme, Lad 1 from Galerina sp. HC1 using a combination of anion exchange- and hydrophobic interaction chromatography. Lad l has a molecular mass of 64 kDa, an isoelectric point of 4, and 3.35 copper atoms/enzyme molecule. The enzyme has features typical of fungal blue laccases. The sequences of two internal peptides were highly similar to reported laccase sequences from other fungi such as Trametes sp. Lad 1 exhibited optimal activity on substrate 2,2'-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) at pH 3 and 60 degrees C. It had high stability at <= 20 degrees C and at high pH. Lad 1 exhibited high substrate affinity and the highest catalytic efficiency reported among laccases for ABTS, and among the lowest for syringaldazine. The most potent inhibitors of Lad 1 were sodium azide, sodium cyanide, disulfide reducing agents, and metal ions in the order Li+ > Sn2+ > Hg2+. The laccase efficiently catalyzed demethylation of eucalyptus hard wood Kraft lignin. (C) 2010 Elsevier Ltd. All rights reserved.",

keywords = "Laccase, Galerina sp., Oxygen consumption, Inhibition, Lignin, Demethylation",

author = "Victor Ibrahim and Laura Mendoza and Gashaw Mamo and Rajni Hatti-Kaul",

year = "2011",

doi = "10.1016/j.procbio.2010.07.013",

language = "English",

volume = "46",

pages = "379--384",

journal = "Process Biochemistry",

issn = "1873-3298",

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TY - JOUR

T1 - Blue laccase from Galerina sp.: Properties and potential for Kraft lignin demethylation

AU - Ibrahim, Victor

AU - Mendoza, Laura

AU - Mamo, Gashaw

AU - Hatti-Kaul, Rajni

PY - 2011

Y1 - 2011

N2 - We purified a laccase isoenzyme, Lad 1 from Galerina sp. HC1 using a combination of anion exchange- and hydrophobic interaction chromatography. Lad l has a molecular mass of 64 kDa, an isoelectric point of 4, and 3.35 copper atoms/enzyme molecule. The enzyme has features typical of fungal blue laccases. The sequences of two internal peptides were highly similar to reported laccase sequences from other fungi such as Trametes sp. Lad 1 exhibited optimal activity on substrate 2,2'-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) at pH 3 and 60 degrees C. It had high stability at <= 20 degrees C and at high pH. Lad 1 exhibited high substrate affinity and the highest catalytic efficiency reported among laccases for ABTS, and among the lowest for syringaldazine. The most potent inhibitors of Lad 1 were sodium azide, sodium cyanide, disulfide reducing agents, and metal ions in the order Li+ > Sn2+ > Hg2+. The laccase efficiently catalyzed demethylation of eucalyptus hard wood Kraft lignin. (C) 2010 Elsevier Ltd. All rights reserved.

AB - We purified a laccase isoenzyme, Lad 1 from Galerina sp. HC1 using a combination of anion exchange- and hydrophobic interaction chromatography. Lad l has a molecular mass of 64 kDa, an isoelectric point of 4, and 3.35 copper atoms/enzyme molecule. The enzyme has features typical of fungal blue laccases. The sequences of two internal peptides were highly similar to reported laccase sequences from other fungi such as Trametes sp. Lad 1 exhibited optimal activity on substrate 2,2'-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) at pH 3 and 60 degrees C. It had high stability at <= 20 degrees C and at high pH. Lad 1 exhibited high substrate affinity and the highest catalytic efficiency reported among laccases for ABTS, and among the lowest for syringaldazine. The most potent inhibitors of Lad 1 were sodium azide, sodium cyanide, disulfide reducing agents, and metal ions in the order Li+ > Sn2+ > Hg2+. The laccase efficiently catalyzed demethylation of eucalyptus hard wood Kraft lignin. (C) 2010 Elsevier Ltd. All rights reserved.

KW - Laccase

KW - Galerina sp.

KW - Oxygen consumption

KW - Inhibition

KW - Lignin

KW - Demethylation

U2 - 10.1016/j.procbio.2010.07.013

DO - 10.1016/j.procbio.2010.07.013

M3 - Article

SN - 1873-3298

VL - 46

SP - 379

EP - 384

JO - Process Biochemistry

JF - Process Biochemistry

IS - 1

ER -

Blue laccase from Galerina sp.: Properties and potential for Kraft lignin demethylation

Abstract

Subject classification (UKÄ)

Free keywords

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