Decolorization of Synthetic Dyes by Ficus carica Latex Peroxidase Isoenzymes
Alshaimaa M. Elsayed, Usama M. Hegazy, Marwa G. A. Hegazy, Somia S. Abdel-Ghany, Walaa H. Salama, Ahmed M. H. Salem, Afaf S. Fahmy
Biotechnology Journal International · pp. 1–14 · Published 26 Jul 2018
10.9734/BJI/2018/42682Abstract
Aims: The current study aims to elucidate the potential of Ficus carica latex peroxidase isoenzymes for decolorizing different synthetic dyes in comparison to the commercial horseradish peroxidase. Study Design: The decolorization of 20 dyes was investigated using the purified F. carica latex peroxidase isoenzymes (purified FP1 and partially purified FP2, and FP3), and horseradish peroxidase (HRP) as a control. Place and Duration of Study: Molecular Biology Department, Genetic Engineering and Biotechnology Research Division, National Research Centre, Egypt, between January 2017 and March 2018. Methodology: The purified and partially fractions of peroxidase isolated from latex of F. carica were used for the present study. Stock solutions of the dyes were prepared in 0.05 M sodium acetate buffer (pH 5.5) and diluted to the requested concentrations ranged from 12 to 330 µM in order to get maximum absorbance does not exceed 1.5 as initial reading. The efficiency of decolorization was expressed in terms of percentage. All experiments were performed in triplicate. Results: F. carica latex peroxidase isoenzymes and commercial horseradish peroxidase were able to decolorize some of tested dyes and the extent of decolorization achieved with different dyes classes were varied according to different chemical structure of each dye. The decolorization efficiency after 3 h of incubation at 40°C using 6.4 U/ml of peroxidase activity of FP1, FP2, FP3 and HRP, was found to be extremely efficient in decolorizing some dyes and relatively low in other dyes. Conclusion: The efficiency of F. carica latex peroxidase isoenzymes toward different synthetic dyes meet the prerequisites needed for environmental and industrial applications.
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