Purification and Characterization of Laccase Secreted by L. lividus

Abstract

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.

Genome-wide inventory of metal homeostasis-related gene products including a functional phytochelatin synthase in the hypogeous mycorrhizal fungus Tuber melanosporum

“…5). In keeping with this view, some MCOs have been shown to act as cell wall-associated ectoenzymes (Sahay et al, 2009). It is interest- ing to note, in this regard, the presence of a putative secretion signal peptide in the N-terminal region of TmelLcc1 (aa 1-23).…”

Optimization of the production, purification and characterization of a laccase from the native fungus Xylaria sp.

“…However, it is important to underscore that the yield obtained for the purification process in different reports, which apply different strategies, is highly variable and is related to the specific characteristics for each crude extract and enzyme. Among this variability, excellent yields such as 77.6% have been obtained by Patel et al, (2014) working with P. ostreatus, but low yields have been reported by other researchers such as Sahay et al, (2008) with 3,46% yield using Pleorotus sajor-caju MTCC 141; or Diaz et al, (2010) with 2,2 and 2,6% yield for laccase isoforms I and II from Coriolopsis rigida; or Junghans et al, (2009) with 0,95% yield using Phoma sp. In contrast, the specific activity value obtained in this study was superior to the activity value obtained for the purified enzymes from other organisms.…”

Laccase oxidation and removal of toxicants released during combustion processes

“…3). Therefore the type of analytical methods used could be the reason for the controversy regarding the ability of laccase to oxidize m-cresol with some groups reporting no oxidation (Zouari-Mechichi et al, 2006;Sahay et al, 2009). HPLC analysis showed that laccase was able to oxidize 47% w/v of m-cresol, 100% of p-cresol and o-cresol and 64% w/v resorcinol in 5 min.…”