Extraction and purification techniques of the bio-catalyst cabbage peroxidase enzyme to remove reactive dyes and bisphenol-A pollutants

Abstract

The industrial dyes and phenols resulting from various industries have a devastating impact on human health and the ecosystem when they enter the food chain, making it necessary to research effective and sustainable treatments. This study informs a novel resource of peroxidase, extracted from discarded cabbage stems purchased from restaurant garbage to use as a biocatalyst treatment. The research focused on comparing the effectiveness of crude and purified enzymes for biodegrading dyes and bisphenol-A. The purification fold for Cabbage legs peroxidase (CLP) was 2.14 with a 39 % yield. At pH 6 and 40 °C the optimum activity of the enzyme was observed, and from its initial activity, the retention is 65% at 60 °C. The (CLP) has been assessed by determining the Michaelis-Menten constant Km value for pyrogallol and H2O2, which were found to be 0.78 mM and 0.047 mM, respectively. For RB49 and RG19 the percentage decolorization was 86% and 78%, respectively after 10-h incubation. The pure enzyme concurrently displayed 79% and 75% decolorization percentages for RB49 and RG19 at the same time and conditions. The crude enzyme demonstrated outstanding effectiveness in removing pollutants. The results indicate that (CLP) holds a promising potential for environmental remediation and bioengineering problems.

Keywords

• Biocatalyst enzyme
• Bisphenol-A
• Cabbage legs peroxidase
• Characterization
• Decolorization and degradation
• Textile dyes