Caralluma umbellata Peroxidase: Biochemical Characterization and Its Detoxification Potentials in Comparison with Horseradish Peroxidase

• Published in: Applied biochemistry and biotechnology 2017-02, Vol.181 (2), p.801-812
• Main Authors: Achar, Raghu Ram, Venkatesh, B. K., Vivek, H. K., Priya, B. S., Swamy, S. Nanjunda
• Format: Article
• Language: English
• Subjects: Apocynaceae - classification; Apocynaceae - enzymology; Biocatalysts; Biochemistry; Biodegradation; Biodegradation, Environmental; Bioremediation; Biotechnology; Chemistry; Chemistry and Materials Science; Coloring Agents - chemistry; Coloring Agents - isolation & purification; Detoxification; Enzyme Activation; Enzyme Stability; Hazardous materials; Horseradish Peroxidase - chemistry; Hydrogen peroxide; Peroxidase - chemistry; Phenols; Phenols - chemistry; Phenols - isolation & purification; Species Specificity; Substrate Specificity; Water Pollutants, Chemical - chemistry; Water Pollutants, Chemical - isolation & purification; Water Purification - methods
• ISSN: 0273-2289; 1559-0291
• DOI: 10.1007/s12010-016-2250-1

Caralluma umbellata peroxidase (CUP) is an acidic heme-containing protein having a molecular weight of ~42 kDa and is specific to guaiacol. It is not a glycoprotein. It was purified to 12.5-fold purity with 6.16 % yield. Its activity is dependent on hydrogen peroxide and has an optimum pH and temperature of 6.2 and 45 °C respectively. It can decolorize dyes, viz., Aniline Blue, Reactive Black 5, and Reactive Blue 19 but not Congo Red, while HRP can decolorize Congo Red also. It has lignin-degrading potentiality as it can decompose veratryl alcohol. Detoxification of phenol was more by CUP compared to HRP while with p -nitrophenol HRP has a greater detoxification rate. Based on our results, CUP was identified to be capable of oxidizing a variety of hazardous substances and also a lignin-degrading plant biocatalyst.