Characterization and kinetic properties of the purified trematosphaeria mangrovei laccase enzyme.

Abstract

The properties of Trematosphaeria mangrovei laccase enzyme purified on Sephadex G-100 column were investigated. SDS—PAGE of the purified laccase enzyme showed a single band at 48 kDa. The pure laccase reached its maximal activity at temperature 65 °C, pH 4.0 with K,,, equal 1.4 mM and Vn.,„„ equal 184.84 U/mg protein. The substrate specificity of the purified laccase was greatly influ¬enced by the nature and position of the substituted groups in the phenolic ring. The pure laccase was tested with some metal ions and inhibitors, FeSO4 completely inhibited laccase enzyme and also highly affected by (NaN3) at a concentration of 1 mM. Amino acid composition of the pure enzyme was also determined. Carbohydrate content of purified laccase enzyme was 23% of the enzyme sam¬ple. The UV absorption spectra of the purified laccase enzyme showed a single peak at 260-280 nm.