Blue Copper Peroksidase and Phthalocyanine Conjugate: Synthesis, Characterization and Applications.

Trametes versicolor can degrade barks as a source for carbon necessity. Therefore it secretes lignin peroxidase, mangan peroxidase and laccase. The laccase enzyme was produced high yield at pH and glucose concentration 5 and 10 gL-1, respectively. In optimized medium, the enzyme activity was between 200-250 UL-1 when inducer was absent. It was seen that the activity reached 400 UL-1 when phenol used as an inducer. The molecular weight of purified laccase was found 80 kDa with SDS-PAGE and kinetic constant Km and Vmax values for ABTS were determined 3.66x10-4 μM and 1652 UL-1, respectively. Hence, due to these properties, these enzymes are widely used in industrial areas free or immolized. Laccase enzyme decolorization of 6 different dyes was carried out. A decolorization capacity of 50-99% was achieved by cultivation in 20 days using a beginning dye concentration of 20 ppm. The removal of color with active enzyme is obtained around 90%. Also laccase enzyme was conjugated amine functionalized low symmetrically phthalocyanine. This conjugate was examined both photodynamic therapy and chemosensor application. This conjugate fluorescence had a quantum yield of 0.32 (lifetime 3.59 ns) and generates efficiently singlet oxygen (quantum yield 0.4). The conjugate was successfully photodamage displayed in HeLa and HuH-7 cells in photodynamic therapy application. These results indicate that conjugate represent interesting agent with potential applications in photodynamic therapy. In addition that the chemosensor behavior of this compound to different metal ions has been studied and this conjugate display as fluorescence chemosensor for determination of Fe3+ions.