CD Skripsi
Uji Aktivator dan Inhibitor Beberapa Ion Logam Terhadap Aktivitas Enzim Lakase A dan B Trichoderma Asperellum LBKURCC1
Laccase (E.C1.10.3.2 : oxygen oxidoreductase) is a multi-copper enzyme that catalyzes oxidation process or release of substrate electrons using oxygen molecules as electron acceptors. Laccase used in this study came from Trichoderma asperellum LBKURCC1. The purpose of this study was to analyze the effect of metal ions (Cu2+, Co2+, Zn2+, Mn2+, Mg2+, and Fe2+) on the activity of laccase A and B, which are resulting in two laccase by T. asperellum LBKURCC1 with different activities and purity levels. The test of the effect of metal on the two laccase preparations was tested with two variations concentration, namely 0,5 mM and 5 mM. The fraction that has higher activity and purity is called laccase A and the fraction that has lower activity and lower purity is called laccase B. The activity of the laccase enzyme was tested using substrates 2,2'-azinobis-3- ethylbenzothiazoline- 6-acid sulfonate (ABTS) measured at a wavelength of 405 nm using a microplate reader. In previous studies, the optimum pH and temperature of laccase were 5.5 and 45ºC. The activity of laccase A is 163,043±5,43 U / L. The activity of laccase A could be increased significantly (p< 0.05) by the addition of Cu2+ ion concentration of 0.5 mM (297±19)% control and of 5 mM (407±80)% control. Laccase A activity also increased significantly (p< 0.05) by the addition of Co2+ 0.5 mM (180±14)% control and 5 mM (115±7)% control. Laccase B activity is 144,02±2,71 U/L, laccase B activity could be increased significantly (p< 0.05) by the addition of Cu2+, Co2+, Fe2+ and Mg2+ metal ions with the concentration of 5 mM (445±59% control, 434±5,33% control, 155±27% control and 219±50% control).
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