Laccases are multicopper oxidases (E.C. 1.10.3.2) that catalyze the oxidation of many phenolic compounds. In this study, a novel laccase, Stlac4, from Setosphaeria turcica was cloned and expressed in Escherichia coli by insertion into the pET-30a expression plasmid. The recombinant laccase was purified and visualized on SDS-PAGE as a single band with an apparent molecular weight of 71.5 KDa, and confirmed by Western blot. The maximum activity of the purified laccase was 127.78 U · mg −1 , the optimum temperature and pH value were 60°C and 4. Laccases are wide-spread in nature and over 220 species of laccases have been isolated from many sources,including plants, fungi, bacteria, and insects [3][4][5][6][7]. Fungal laccases are the most extensively studied multicopper oxidases, and while primarily considered to be involved in lignin degradation [8], recent studies have shown that fungal laccases participate in fruiting body formation [9], pigment biosynthesis [10], pathogenesis, and stress defense [11]. Laccases are also very important and valuable enzymes for various biotechnological and industrial applications, such as biodegradation of lignin without polluting the environment, degradation of recalcitrant compounds, environmental protection and bioremediation, biological bleaching in the paper industry, and textile dye decolorization [12,13]. Several laccase genes have been cloned from different fungal sources and heterologously expressed with the specific purpose of using laccases more efficiently in biotechnology. Like other enzymes, laccases often face harsh conditions in industrial processes, such as high temperature, high salt concentration, and extremely acidic or alkaline pH [14,15]. Identification of laccase enzymes robust to harsh conditions could improve economic viability of this process. The majority of fungal laccases operate in the range of 30-55°C, and their optimal pH range is limited to mildly acidic conditions [16]. Many strategies Shuangxin Ma and Ning Liu contributed equally to this work.68 |