Abstract:
Laccase are extracellular enzymes containing metal ions which used oxygen compounds to
catalyze the oxidations process of various aromatic and nonaromatic compounds. The purpose of
the study was to purify and determining laccase spesific activity from the isolate fungus T.
asperellum LBKURCC1. Laccase enzymes purification process was carried out by teo steps, that
was fractionation with ultrafiltraton membranes 10.000 MWCO (Molecular Weight Cut Of) and
saturated with the addition of ammonium sulfate salts with saturation variations of 0-20%, 20-
40%, 40-60% and 60-80%. Based on this research, the results obtained were the activity of crude
extract laccase of 0,01955 U/L, and highest enzymes activity was the enzyme purified by
ammonium sulfat salt 0-20% saturation fraction of 0,03055 U/L. Specific activity of crude
extract laccase enzyme was obtained at 4,4353 U/mg and the specific activity of purified
enzymes decreased 2,1962 U/mg with a yield of 157,1296%. The results showed that enzymes in
the saturation fraction of 0-20% ammonium sulfate was high activity and purity.
