Purification and Characterization of Laccase Secreted by L. lividus

The culture conditions for maximum secretion of laccase by Loweporus lividus MTCC-1178 have been optimized. The laccase from the culture filtrate of L. lividus MTCC-1178 has been purified to homogeneity. The molecular weight of the purified laccase is 64.8 kDa. The enzymatic characteristics like K m...

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Bibliographic Details
Published in:Applied biochemistry and biotechnology 2009-05, Vol.157 (2), p.311-320
Main Authors: Sahay, R, Yadav, R. S. S, Yadav, K. D. S
Format: Article
Language:English
Subjects:
Biochemistry
Biological and medical sciences
Biophysics
Biotechnology
catechol
Chemistry
Chemistry and Materials Science
cresols
Culture Media
Electrophoresis, Polyacrylamide Gel
Enzyme Stability
enzyme substrates
Enzymes
Filtrate
Fundamental and applied biological sciences. Psychology
Fungi
Hydrogen-Ion Concentration
laccase
Laccase - isolation & purification
Laccase - secretion
Loweporus lividus
Molecular Weight
optimization
Polyporaceae - enzymology
protein secretion
purification
pyrogallol
Pyrogallol - analogs & derivatives
Pyrogallol - metabolism
Substrate Specificity
Substrates
syringaldazine
Temperature
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Summary:The culture conditions for maximum secretion of laccase by Loweporus lividus MTCC-1178 have been optimized. The laccase from the culture filtrate of L. lividus MTCC-1178 has been purified to homogeneity. The molecular weight of the purified laccase is 64.8 kDa. The enzymatic characteristics like K m, pH, and temperature optimum using 2,6-dimethoxyphenol have been determined and found to be 480 μM, 5.0, and 60 °C, respectively. The K m values for other substrates like catechol, m-cresol, pyrogallol, and syringaldazine have also been determined and found to be 230, 210, 320, and 350 μM, respectively.
ISSN:0273-2289
1559-0291
DOI:10.1007/s12010-008-8265-5