The laccase has the ability to oxidize substituted phenols and the water is the sole byproduct, thus it has been employed to remove and/or modify the lignin in lignocellulosic material. A putative laccase gene, LacSM, from Sordaria macrospora k-hell was screened by a genome mining approach. Then, it was cloned and highly expressed in Escherichia coli. The molecular weight of recombinant LacSM was ~ 67 kDa. The optimal pH values for the LacSM oxidation of guaiacol, syringaldazine, 2,6-dimethoxyphenol, and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) were 6, 7, 5, and 5, respectively. The optimal activity of laccase was observed at 60, 55, 55, and 50 °C for four respective substrates. LacSM remained stable at pH 5-8 and thermostable at 60 °C with guaiacol as the substrate. 1 mM K+, Na+, or Mn2+ ions slightly stimulated laccase activity. In addition, LacSM was moderately tolerant to the Cl- ion and showed an ability to remove and/or modify lignin. Thus, LacSM was a potential candidate for industrial applications, such as lignin degradation of lignocellulosic biomass.