Abstract
The large family of enzymes, known as polyphenols oxidases, includes laccase. Due to the inclusion of a copper atom in their catalytic core, laccases are frequently referred to as multi-copper oxidases. Laccases are versatile enzymes that can catalyze the oxidation of a wide range of phenolic and non-phenolic substances. In the current study, a local strain of Aspergillus niger was used for solid-state fermentation to produce fungal laccase, as well as purify and optimize laccase. The enzyme profile, which was acquired using guaiacol to measure enzyme activity, showed that after five days of incubation, wheat straw provided the highest level of laccase activity, or 2.551 U/mL. A technique called response surface methodology (RSM) was used to examine the effects of various conditions on the production of enzymes. The RSM results demonstrated that after five days of incubation, the enzyme activity was at its highest at 45 degrees C, pH 5.5, and 30% moisture level, inoculated with 2 mL mycelium. Through ammonium sulphate precipitation and dialysis, the enzyme was purified. Additionally, column chromatography was used to further purify laccase. The next step was enzyme characterization to evaluate how temperature and pH affected enzyme activity. At 45 degrees C and pH 5.5, the isolated enzyme produced its highest level of activity. The findings of the current study showed that A. niger is capable of producing laccase in an economical and environmentally friendly way. Due to its unique oxidative and catalytic features, this enzyme has received a lot of attention recently.