Azo dyes, the most commonly used industrial textile dyes, are carcinogenic, mutagenic, notoriously difficult to degrade, and persist in the environment; thus, newer and greener methods are needed to degrade azo textile dyes. The current study compared the ability of horse heart myoglobin and horse hemoglobin to degrade the azo dyes Reactive Black 5, Amaranth, Evans Blue, Black Diamond, Eriochrome Black T and Xylidine Ponceau with hydrogen peroxide by monitoring the reaction progress with UV-Vis spectrophotometry. Michaelis-Menten kinetics was then used to calculate the kinetic parameters and determine the kcat values. The results indicate that both proteins demonstrate promise as green catalysts, although horse hemoglobin is the faster, more efficient choice of the two. For instance, hemoglobin degradation of Reactive Black 5 with H2O2 is 12-fold faster than with myoglobin. The apparent dissociation constant, KM, is greater for hemoglobin (31 0.35 µM ) than myoglobin (16 1.78 µM). Thus the catalytic efficiency of hemoglobin in degrading Reactive Black is approximately 7-fold greater than myoglobin. The kinetic results for all studied azo dyes, as well as degradation products from gas chromatography-mass spectrometry and liquid chromatography-mass spectrometry to better understand the azo dye degradation reaction and potential mechanism, will be presented.

Potential of horse hemoglobin and horse heart myoglobin as green catalysts in the degradation of industrial textile azo dyes with hydrogen peroxide

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