Purification and Characterization Laccase from Trametes versicolor (L.) Lloyd in Submerged Fermentation.

Abstract

<b>Background and Objective:</b> Laccase is classified as an oxidoreductase enzyme that catalyzes oxidation reactions of phenolic groups by using oxygen as its electron acceptor. Laccase isolated from <i>Trametes versicolor</i> (L.) Lloyd has a wide range of applications in the industrial sector. The use of enzymes in the industrial sector requires pure enzyme conditions from impurities so that the enzyme can maximize its ability in converting the substrate. This study aims to obtain enzyme activity and the characteristic of purified laccase enzymes isolated from <i>Trametes versicolor</i> (L.) Lloyd. <b>Materials and Methods:</b> This study was conducted with an experimental method followed by descriptive analysis. The steps of this research consist of a qualitative assay of laccase enzyme, crude laccase extract desalting by Sephadex G-25, laccase purification by Sephadex G-100 and laccase optimum pH characterization. <b>Results:</b> The result of this study showed that purification of laccase from <i>Trametes versicolor </i>(L.) Lloyd with Sephadex G-25 increases laccase enzyme-specific activity which is 10.966 U mg<sup>1</sup> and reaches 2.93-fold purity. The highest laccase enzyme activity was achieved at pH 4 with a value of laccase activity 62.39 U L<sup>1</sup>. <b>Conclusion:</b> Based on current results, purifying laccase from <i>Trametes versicolor </i>(L.) Lloyd with Sephadex G-25 was recommended which resulting higher enzyme specific activity.