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

Achar, Raghu Ram and Venkatesh, B. K. and Vivek, H. K. and Priya, B. S. and Nanjunda Swamy, S. (2017) Caralluma umbellata Peroxidase: Biochemical Characterization and Its Detoxification Potentials in Comparison with Horseradish Peroxidase. Applied Biochemistry and Biotechnology, 181 (2). pp. 801-812. ISSN 1559-0291

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Official URL: https://doi.org/10.1007/s12010-016-2250-1

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.

Item Type: Article
Subjects: C Chemical Science > Chemistry
Divisions: Department of > Chemistry
Depositing User: C Swapna Library Assistant
Date Deposited: 25 Jun 2019 10:22
Last Modified: 08 Jul 2022 06:38
URI: http://eprints.uni-mysore.ac.in/id/eprint/3835

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