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ISSN: 2157-7048

Journal of Chemical Engineering & Process Technology
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Research Article

Isolation,Partial Purification and Characterization of Phospholipid Hydroperoxide Glutathione Peroxidase(Phgpx Enzyme from Oryza Sativa Seedlings

Om Prakash Verma1*, Pankaj Kumar Ojha1, Shashi B Bailey1, Pankaj Singh1, Rajendra Dubey2 and B.N.Mishra3
1Jacob School of Biotechnology & Bioengineering, SHIATS, Allahabad
2Galaxy Concepts Kolkata
3IET, Lucknow
Corresponding Author : Om Prakash Verma
Jacob School of Biotechnology & Bioengineering
Shiats, Allahabad
E-mail: [email protected]
Received September 28, 2011; Accepted November 21, 2011; Published November 25, 2011
Citation: Verma OP, Ojha PK, Bailey SB, Singh P, Dubey R, et al. (2011) Isolation, Partial Purification and Characterization of Phospholipid Hydroperoxide Glutathione Peroxidase (Phgpx Enzyme from Oryza Sativa Seedlings. J Chem Eng Process Technol 2:120.doi:10.4172/2157-7048.1000120
Copyright: © Verma OP, Ojha PK, Bailey SB, Singh P, Dubey R, et al. (2011) Isolation, Partial Purification and Characterization of Phospholipid Hydroperoxide Glutathione Peroxidase (Phgpx Enzyme from Oryza Sativa Seedlings. J Chem Eng Process Technol 2:120.
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Abstract

The recombinant Phospholipid hydroperoxide glutathione peroxidase isolated from Oryza sativa is a type of antioxidant enzyme. It is stable at pH 7-8 and temperature 27 and 62°C. The molecular weight of enzyme was found to be around 21-26 kDa by SDS PAGE. The peroxidation activity of PHGPx was inhibited by HgCl2, EDTA, Potassium ferrocynate and was activated by FeCl2 and MnSO4 .These properties indicate that the possibilities for use of the PHGPx in the medical, clinical and cosmatic industry. This enzyme can be exploited commercially with some modification.

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