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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.
Index Copernicus ICI Journals Master List 2018 - IJCMAS--ICV 2018: 95.39 For more details click here
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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 2017: 100.00
NAAS RATING 2018: 5.38

Int.J.Curr.Microbiol.App.Sci.2016.5(2): 836-844
DOI: http://dx.doi.org/10.20546/ijcmas.2016.502.095


Physiochemical properties of purified Catalase enzyme from Azolla 
S.Susmitha1, R.Shyamala Gowri2, P.Meenambigai2, R.Ramitha1 and R.Vijayaraghavan3*
1Dept. of Microbiology, Nehru Arts and Science College, T.M.Palayam, Coimbatore,
Tamilnadu, India
2Dept. of Microbiology and Biochemistry, Nadar Saraswathy College of Arts
and Science, Theni, India
3PSG Centre for Molecular Medicine and Therapeutics, PSG Institute of Medical Sciences and Research, Coimbatore, India
*Corresponding author
Abstract:

Enzymes are the reaction catalysts of biological systems which accelerate and direct specific biochemical reactions. Antioxidant enzymes are capable of stabilizing, or deactivating free radicals before they attack cellular components. Catalase catalyzes the reduction of hydroperoxides, thereby protecting mammalian cells against oxidative damage. The aim of the project is to analyze the presence of antioxidant enzyme and to purify the enzyme from the aquatic fern Azolla.  The catalase enzyme presence was confirmed by standard assay procedure and purified through DEAE cellulose and Sephadox G-75 Column chromatography. The purified catalase enzyme was subjected for Molecular weight determination by SDS-PAGE analysis. Since the separated enzyme appeared as a single band, it was concluded that catalase enzyme as tetrameric.  The purified catalase was found about 55,000 Da molecular weight. Maximum enzyme activity observed at pH 7 which was the optimum pH level of the catalase enzyme purified from Azolla and the optimum temperature level was 10°C.

 


Keywords: Antioxidant, Azolla,
catalase,
DEAE-Cellulose, and SDS-PAGE
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How to cite this article:

Susmitha, S., R.Shyamala Gowri, P.Meenambigai, R.Ramitha and   Vijayaraghavan, R. 2016. Physiochemical properties of purified Catalase enzyme from AzollaInt.J.Curr.Microbiol.App.Sci. 5(2): 836-844. doi: http://dx.doi.org/10.20546/ijcmas.2016.502.095