CHARACTERISTICS OF LACCASE ENZYME EXTRACTED FROM Pleurotus sajor caju

Abstract

Extracellular enzymes such as ligninperoxidase (LiP), manganperoxidase (MnP), laccase have been
shown to be capable of degrading and metabolizing persistent aromatic organic compounds such as
dichlorophenol (DCP), dichlorodiphenyltrichloroethane (DDT), dyes and dioxins. These enzymes can
be produced by bacteria, actinomycetes or fungi, in which white rot fungi and fungi that are able to
grow on lignin substrates produce these enzymes the most. Pleurotus oyster mushrooms are capable of
producing the enzyme laccase with high activity and have also been shown to catalyze the degradation
of dioxin isomers. In this study, some results are presented on the extraction and purification of laccase
enzyme from mushroom growing humus and some characteristics of this laccase enzyme. The results
showed that the laccase enzyme activity was highest at the stage of the bag is white by fungus and
reached 108 U/g. The obtained laccase enzyme has a size of about 60 KDa, has a thermal stability of
30oC in 7h, the optimum temperature for the reaction is 30
oC, the optimal pH is pH5 and has a stability
of pH is 5 for 7h. Enzymes have an alpha helix structure, with 4 copper atoms in the molecule. This
study result showed that crude enzyme was capable of degrading up to 44,79% of total toxicity of
dioxin with initial concentration of 9623 pg/ml.