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

<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 mg¹ 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 L¹. <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.

Potential of Lignocellulosic Waste for Laccase Production by Trametes versicolor under Submerged Fermentation.

<b>Background and Objective:</b> Laccase is one of the ligninolytic enzymes classified as a multicopper oxidoreductase group that has the ability in oxidizing phenolic compounds and has widespread use in both food and non-food industries. This enzyme is extracellularly secreted by white-rot fungi, <i>Trametes versicolor</i> (L.) Lloyd in the media containing lignocellulose, for example, kapok banana peels and sawdust. The objective of this study was to evaluate lignocellulosic substrate that able to produce the highest activity of the laccase from the <i>T. versicolor </i>(L.) Lloyd. <b>Materials and Methods:</b> Three substrate variations used in this work included the cultivation media with the addition of either kapok banana peels or sawdust and without using both materials. The inducer (CuSO₄) was added to each substrate variation and the laccase activity was subsequently measured. <b>Results:</b> The qualitative test result for laccase detection showed that <i>T. versicolor </i>(L.) Lloyd<i> </i>was able to produce this enzyme indicated with a reddish-brown surrounding fungal colony. The fungi cultivated in media with the content of sawdust and 1 mM CuSO₄ yielded the highest laccase activity, reaching 573.6 U L¹ with an OD value of 0.5567<i> </i>and a pH of 5.3 after 7 days of incubation. Meanwhile, the addition of kepok banana peels and 1 mM CuSO₄, showed the maximum laccase activity (297.7 U L¹) with the OD value of 0.6932 and a pH of 5 after incubation for 6 days. <b>Conclusion:</b> The white-rot fungi of <i>T. versicolor</i> (L.) Lloyd<i> </i>could produce optimal laccase activity by adding sawdust substrate and 1 mM CuSO₄inducer on submerged fermentation.