Caralluma umbellata Peroxidase: Biochemical Characterization and Its Detoxification Potentials in Comparison with Horseradish Peroxidase
| Autor: | B. K. Venkatesh, Raghu Ram Achar, B. S. Priya, S. Nanjunda Swamy, H. K. Vivek |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Bioengineering 010501 environmental sciences 01 natural sciences Applied Microbiology and Biotechnology Biochemistry Horseradish peroxidase Substrate Specificity Water Purification 03 medical and health sciences chemistry.chemical_compound Phenols Species Specificity Detoxification Enzyme Stability Oxidizing agent Phenol Organic chemistry Coloring Agents Hydrogen peroxide Molecular Biology Horseradish Peroxidase Peroxidase 0105 earth and related environmental sciences biology fungi food and beverages General Medicine Congo red Apocynaceae Enzyme Activation Biodegradation Environmental 030104 developmental biology chemistry biology.protein Guaiacol Water Pollutants Chemical Biotechnology Nuclear chemistry |
| Zdroj: | Applied Biochemistry and Biotechnology. 181:801-812 |
| ISSN: | 1559-0291 0273-2289 |
| DOI: | 10.1007/s12010-016-2250-1 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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