Purification and enzymatic properties of a textile dye-decolourizing peroxidase from Moringa oleifera roots / Purificação e propriedades enzimáticas de uma peroxidase descorante de corantes têxteis a partir de raízes de Moringa oleifera

Marina Gabrielle Guimarães de Almeida, Larissa Alves Lopes, Lucas Pinheiro Dias, Helen Paula Silva da Costa, Celso Shiniti Nagano, Rômulo Farias Carneiro, Ilka Maria Vasconcelos, Daniele de Oliveira Bezerra de Sousa

Abstract


Peroxidases are ubiquitous enzymes involved in the oxidation of a variety of aromatic substrates including textile dyes, which are harmful for aquatic life and human health. Hence, the present study describes the purification of a peroxidase, named MoPOX, from Moringa oleifera roots using DEAE-Sephacel and gel filtration chromatography on a Superdex® 75 column. The peptide sequences recorded by mass spectrometry analysis confirmed the identity of MoPOX with other plant peroxidases. The optimum pH and temperature of enzyme activity were 5.2 and 70 °C, respectively. Its enzymatic activity in the presence of metal ions and classical peroxidase inhibitors was also evaluated. MoPOX follows Michaelis-Menten kinetics, with specificity, in ascending order, to the substrates ABTS < eugenol < O-dianisidine ≅ guaiacol, besides being highly thermostable. The purified peroxidase (0.015, 0.030 or 0.150 mg/mL) degraded different dyes (50 or 100 mg/L), such as Remazol® Blue RGB, Remazol® Navy RGB and Telon® Turquoise M-5G 85%. Decolorization rates varied from 15 to 90% depending on the dye concentration, enzyme concentration and exposure time. MoPOX is the first peroxidase purified from M. oleifera roots, and the results showed it has biotechnological potential for biodegradation of hazardous compounds.

 


Keywords


Plant peroxidase, textile dye, Moringa oleifera, bioremediation.

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DOI: https://doi.org/10.34117/bjdv6n4-066

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