Abstract
In this study, the Production of laccase enzyme from Trametes hirsuta strain (DSMZ No.5072) in the 2L fermenter using different culturing media had been achieved. The production of laccase was also induced by using different concentrations of Copper sulphate, 2, 5 Xylidine and Gallic acid as inducers. The maximum laccase activitiy observed during T. hirsuta growth in the presence of various inducers was 5.89 U ml -1. Laccase purification was performed by precipitated the enzymes with ammoniam sulphate, saturation 90%, followed by gel filtration chromatography using Sephadex-G25 and more purified by ion-exchanger (DEAE-Sephadex). The obtained enzyme was concentrated by ultra filtration membrane and analyzed by SDS-PAGE. The activity of home prepared laccase and the commercial laccase from Trametes versicolor were carried out in different media (aqueous, reverse micelles, co-solvent, ionic liquid and ternary systems) depend on oxidation of ABTS as an enzyme substrate. The optimum pH for the laccase activity of the two fungal laccases was observed at acidic pH values close to (pH 3.5-4.6) while the optimum temperature was 70ºC.
Highlights
Laccase is one of the very few enzymes that have been studied since the end of 19th century
No oxidation of 2-propanol was detected in all reaction systems used. 3.2 Catalytic activity of laccase entrapped in Reverse Micelles (RMs) In an effort to utilize laccase in an organic solvent, a homogeneous aqueous-organic mixture system, combination of water and Bis-2-ethylhexyl sulfosuccinate sodium salt (AOT) was investigated as media for laccase activity, using as role model reaction the oxidation of ABTS
Based on the results present in Table (4), it was found that AOT reversed micellar system is a suitable environment for the two fungal laccase to retain its catalytic activity
Summary
Abstrac : In this study, the Production of laccase enzyme from Trametes hirsuta strain (DSMZ No.5072) in the 2L fermenter using different culturing media had been achieved. The production of laccase was induced by using different concentrations of Copper sulphate, 2, 5 Xylidine and Gallic acid as inducers. Laccase purification was performed by precipitated the enzymes with ammoniam sulphate, saturation 90%, followed by gel filtration chromatography using Sephadex-G25 and more purified by ionexchanger (DEAE-Sephadex). The activity of home prepared laccase and the commercial laccase from Trametes versicolor were carried out in different media (aqueous, reverse micelles, co-solvent, ionic liquid and ternary systems) depend on oxidation of ABTS as an enzyme substrate. The optimum pH for the laccase activity of the two fungal laccases was observed at acidic pH values close to (pH 3.5-4.6) while the optimum temperature was 70?C
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