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

Ibrahim, Victor LU ; Mendoza, Laura LU ; Mamo, Gashaw LU and Hatti-Kaul, Rajni LU (2011) In Process Biochemistry 46(1). p.379-384
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... (More)
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. (Less)
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organization
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Contribution to journal
publication status
published
subject
keywords
Laccase, Galerina sp., Oxygen consumption, Inhibition, Lignin, Demethylation
in
Process Biochemistry
volume
46
issue
1
pages
379 - 384
publisher
Elsevier
external identifiers
  • wos:000286538300053
  • scopus:78650238979
ISSN
1873-3298
DOI
10.1016/j.procbio.2010.07.013
language
English
LU publication?
yes
id
2134e015-bb39-4158-a493-d6a8748b7650 (old id 1878257)
date added to LUP
2011-04-07 11:52:30
date last changed
2017-09-24 03:18:48
@article{2134e015-bb39-4158-a493-d6a8748b7650,
  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 &lt;= 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+ &gt; Sn2+ &gt; Hg2+. The laccase efficiently catalyzed demethylation of eucalyptus hard wood Kraft lignin. (C) 2010 Elsevier Ltd. All rights reserved.},
  author       = {Ibrahim, Victor and Mendoza, Laura and Mamo, Gashaw and Hatti-Kaul, Rajni},
  issn         = {1873-3298},
  keyword      = {Laccase,Galerina sp.,Oxygen consumption,Inhibition,Lignin,Demethylation},
  language     = {eng},
  number       = {1},
  pages        = {379--384},
  publisher    = {Elsevier},
  series       = {Process Biochemistry},
  title        = {Blue laccase from Galerina sp.: Properties and potential for Kraft lignin demethylation},
  url          = {http://dx.doi.org/10.1016/j.procbio.2010.07.013},
  volume       = {46},
  year         = {2011},
}