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International Journal of Current Microbiology and Applied Sciences (IJCMAS)
IJCMAS is now DOI (CrossRef) registered Research Journal. The DOIs are assigned to all published IJCMAS Articles.
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National Academy of Agricultural Sciences (NAAS)
NAAS Score: *5.38 (2019)
[Effective from January 1, 2019]
For more details click here

ICV 2018: 95.39
Index Copernicus ICI Journals Master List 2017 - IJCMAS--ICV 2018: 95.39
For more details click here

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Original Research Articles

PRINT ISSN : 2319-7692
Online ISSN : 2319-7706
Issues : 12 per year
Publisher : Excellent Publishers
Email : editorijcmas@gmail.com / submit@ijcmas.com
Editor-in-chief: Dr.M.Prakash
Index Copernicus ICV 2018: 95.39
NAAS RATING 2020: 5.38

Int.J.Curr.Microbiol.App.Sci.2018.7(6): 328-339
DOI: https://doi.org/10.20546/ijcmas.2018.706.037


Characterization and Immobilization of Peroxidase Extracted from Horse Radish and Decolorization of Some Dyes
Ali J.R. AL-Sa'ady1, Maha Hameed A. Al-Bahrani2 and Ghazi M. Aziz1
1Department of Biotechnology, College of Science, University of Baghdad, Iraq
2Molecular and Medical Biotechnology Dept. College of Biotechnology, University of Al-Nahrain, Iraq
*Corresponding author
Abstract:

The present work was undertaken to obtain crude Peroxidase extract from radish to characterize it in terms of pH, temperature, number of times use and decolrization of some dyes. The results shows that peroxidase from radish gave highest specific activity 4391 U/mg, and potassium phosphate buffer (0.1 M, pH 7) was best extraction buffer for peroxidase extraction from radish with specific activity 4489 U/mg, while The highest specific activity was measured for crude extract at 1:2 ratio, it was 4479 U/mg protein. Entrapment of peroxidase enzyme by agarose was best method for immobilization. The optimum pH of free and immobilized peroxidase enzyme activity was 6.0, while the pH stability of free peroxidase enzyme from radish was 6.0, and the pH stability of immobilized peroxidase enzyme was range from 4.0-8.0. The optimum temperature for free peroxidase activity from radish was 35 á´¼C, while the free enzyme was stable in temperature 35-60 áµ’C, then the activity begun to decrease and was completely lost in 65-70áµ’C. The best temperature for immobilized peroxidase activity was 35 áµ’C, while the results showed that the immobilized enzyme was stable in temperatures between 35-45 áµ’C. The activity of the immobilized enzyme which incubated many times with substrate was decreased after eighth time using. Giemsa stain and acridine orange, were removed and make change in their absorbance after incubation with immobilized eighth enzyme for period of time, while no degradation of the other dyes occur.


Keywords: Peroxidase, Horseradish, Immobilization, Optimization, Decolorization
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How to cite this article:

Ali J.R. AL-Sa'ady, Maha Hameed A. Al-Bahrani and Ghazi M. Aziz. 2018. Characterization and Immobilization of Peroxidase Extracted from Horse Radish and Decolorization of Some Dyes.Int.J.Curr.Microbiol.App.Sci. 7(6): 328-339. doi: https://doi.org/10.20546/ijcmas.2018.706.037