Caralluma umbellata Peroxidase: Biochemical Characterization and Its Detoxification Potentials in Comparison with Horseradish Peroxidase
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- 作者：Raghu Ram Achar ; B. K. Venkatesh ; H. K. Vivek…
- 关键词：Caralluma umbellata ; Peroxidase ; Dye decolorization ; Detoxification ; Phenol degradation ; Bioremediation
- 刊名：Applied Biochemistry and Biotechnology
- 出版年：2017
- 出版时间：February 2017
- 年：2017
- 卷：181
- 期：2
- 页码：801-812
- 全文大小：
- 刊物类别：Chemistry and Materials Science
- 刊物主题：Biotechnology; Biochemistry, general;
- 出版者：Springer US
- ISSN：1559-0291
- 卷排序：181
文摘
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.