Abstract:
Laccase Trichoderma asperellum LBKURCC1 has been partially purified
fractionation using ammonium sulfate at 0-80% saturation then gel filtration
chromatography. The results of the gel filtration have different activities and
purity levels The fraction has lower activity and lower purity is called laccase flow
through gel filtration chromatography. 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. The
activity of laccase flow through is 144,02±2,71 U/L. The laccase activity was
increased significantly (p≤ 0.05) to (362 ± 48)% and (445 ± 59)% compared to
controls, when the enzyme was incubated for 10 minutes with 0.5 mM and 5 mM
Cu2+ respectively. A significant increase (p≤ 0.05) in laccase activity was also
observed when the enzyme was incubated for 10 minutes in 0.5 mM and 5 mM
Mg2+, The laccase activity was increased significantly (p≤ 0.05) to (343 ± 59)%
and (219 ± 50)% compared to controls.
