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Expression, purification, and characterization of a novel laccase from Setosphaeria turcica in Eschericha coli.
Journal of Basic Microbiology 2018 January
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 4.0 respectively, measured by oxidation of 2,2'-Azinobis-(3-ethylbenzthiazoline-6-sulphonate) (ABTS). Purified laccase activity under different metal ions and an inhibitor were tested, revealing that laccase activity increased by approximately 434.8% with Fe3+ , and 217.4% with Cu2+ at 10 mmol · L-1 concentrations, Mn2+ increased the laccase activity only at 5 mmol · L-1 , while Na+ increased activity at 1 mmol · L-1 but inhibited activity at 5 and 10 mmol · L-1 . SDS increased laccase activity at 1 mmol · L-1 , and inhibited activity at 5 and 10 mmol · L-1 .
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