Журнал химической инженерии и технологических процессов

Журнал химической инженерии и технологических процессов
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ISSN: 2157-7048

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

Om Prakash Verma, Pankaj Kumar Ojha, Shashi B Bailey, Pankaj Singh, Rajendra Dubey and B.N.Mishra

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.

Отказ от ответственности: Этот тезис был переведен с использованием инструментов искусственного интеллекта и еще не прошел рецензирование или проверку.
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