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), pH, and temperature optimum using 2,6-dimethoxyphenol have been determined and found to be 480 microM, 5.0, and 60 degrees 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 microM, respectively.
Sahay
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R
Department of Chemistry, D.D.U. Gorakhpur University, Gorakhpur 273 009, India.
Yadav
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Yadav
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D003470:Culture Media; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D042845:Laccase / Q000302:isolation & purification* / Q000378:metabolism*; D008970:Molecular Weight; D011124:Polyporaceae / Q000201:enzymology*; D011748:Pyrogallol / Q000031:analogs & derivatives / Q000378:metabolism; D013379:Substrate Specificity; D013696:Temperature
D003470:Culture Media; D011748:Pyrogallol; C010120:pyrogallol 1,3-dimethyl ether; D042845:Laccase