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Updated: Mar 14, 2026

Catalytic Scavenging of Plant Reactive Oxygen Species In Vivo by Anionic Cerium Oxide Nanoparticles
Published on: August 26, 2018
Caralluma umbellata Peroxidase: Biochemical Characterization and Its Detoxification Potentials in Comparison with
Raghu Ram Achar1,2,3, B K Venkatesh1,2, H K Vivek1
1Department of Biotechnology, JSS Science and Technology University, JSS Technical Institutions Campus, Mysuru, Karnataka, 570 006, India.
Abstract:
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.
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