CD Skripsi
Uji Aktivitas Enzim Lakase Jamur Lecinellum Sp. M.5, Entoloma Cf. Clypeatum M.12 Dan Entoloma Sp. Kh.08 Isolat Taman Nasional Sebangau, Kalimantan Tengah
Laccase enzyme (p-diphenol; dioxygen oxidoreductase, EC 1.10.3.2). is an oxidoreductase enzyme capable of catalyzing the oxidation of various phenolic and non-phenolic compounds using molecular oxygen (O2) as the sole electron acceptor. The group of laccase enzymes have a wide substrate spectrum. Due to this property, laccase has been widely utilized in various industrial processes. It plays an important role in applications such as agriculture and food processing, pesticide degradation,removal of pharmaceutical and cosmetic residues, dye decolorization, and the treatment of wastewater from pulp and paper industries. This study aims to evaluate the laccase activity of three ectomycorrhizal fungal isolates from Sebangau National Park, Central Kalimantan, Lecinellum sp. M.5, Entoloma cf. clypeatum M.12, and Entoloma sp. KH.08, when grown on fermentation medium containing rice straw as a laccase gene inductor. The fermentation process was conducted under submerged conditions (SmF) using a modified production medium, where wheat straw was used to induce laccase gene expression. Enzyme activity after 3 and 6 days fermentation was measured quantitatively using ABTS as the substrate. The results showed that laccase activity was only detected on day 3 in media containing acetate buffer at pH 5.5, with the highest activity recorded in the Lecinellum sp. M.5 isolate at (0.36±0.07) U/L. Although the laccase activity levels were relatively low, the use of rice straw positively influenced laccase production due to its lignin content, but possibly with limited induction capabilities and low need of the products by the ectomycorrhiza, hence no laccase activity was observed after 6 days fermentation.
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