The white-rot fungus Pleurotus ostreatus secretes laccase isozymes with different substrate specificities

Four laccase isozymes (LCC1, LCC2, LCC3 and LCC4) synthesized by Pleurotus ostreatus strain V-184 were purified and characterized. LCC1 and LCC2 have molecular masses of about 60 and 65 kDa and exhibited the same pI value (3.0). Their N termini were sequenced, revealing the same amino acid sequence...

Full description

Saved in:
Bibliographic Details
Published in:Mycologia 2003-11, Vol.95 (6), p.1013-1020
Main Authors: Mansur, Mariana, Arias, María E., Copa-Patiño, José L., Flärdh, María, González, Aldo E.
Format: Article
Language:English
Subjects:
ABTS
Amino acids
Basidiomycota
Biochemistry/Physiology
Enzymes
Fungi
Gels
guaiacol
isozyme
Lignin
N-terminal sequence
Oxidases
phenoloxidase
Pleurotus
Pleurotus ostreatus
Sodium
Trametes
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Four laccase isozymes (LCC1, LCC2, LCC3 and LCC4) synthesized by Pleurotus ostreatus strain V-184 were purified and characterized. LCC1 and LCC2 have molecular masses of about 60 and 65 kDa and exhibited the same pI value (3.0). Their N termini were sequenced, revealing the same amino acid sequence and homology with laccases from other microorganisms. Laccases LCC3 and LCC4 were characterized by SDS-PAGE, estimating their molecular masses around 80 and 82 kDa, respectively. By native isoelectrofocusing, their pI values were 4.7 and 4.5, respectively. When staining with ABTS and guaiacol in native polyacrilamide gels, different specificities were observed for LCC1/LCC2 and LCC3/LCC4 isozymes.
ISSN:0027-5514
1557-2536
DOI:10.1080/15572536.2004.11833017