Study of physicochemical and kinetics features of peroxidase isolated fromhoary cress (Cardaria draba L.)

Authors

  • Nazar Abdulameer Hamzah University of AL-Qadisiya/

Abstract

New peroxidase may be versatile was investigated in different parts of hoary cress. Roots regarded as a rich source of enzyme (2095.23 U mg-1) comparison in other botanical parts. Peroxidase was purified from roots by ammonium sulfate, dialysis and Sephadex G-100 gel filtration, showed final degree of purity and recovery 2.70 and 45.11% respectively. Molecular mass, optimum of pH, temperature and time of enzymatic reaction were 56.234 kDa, 6.5, 40oC, 3 min. respectively. Km and Vmax were estimated of each substrate (guaiacol and hydrogen peroxide), noticed high affinity to hydrogen peroxide. Competitive sodium azide inhibitor was suppressed peroxidase totally at 90 mM.

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Author Biography

Nazar Abdulameer Hamzah, University of AL-Qadisiya/

College of Science

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Published

2013-04-10

How to Cite

Hamzah, N. A. (2013). Study of physicochemical and kinetics features of peroxidase isolated fromhoary cress (Cardaria draba L.). Al-Kufa University Journal for Biology, 5(1). Retrieved from https://journal.uokufa.edu.iq/index.php/ajb/article/view/7822

Issue

Vol. 5 No. 1 (2013): Magazine of Al-kufa University for Biology.

Section

Articles

License

Copyright (c) 2013 Nazar Abdulameer Hamzah

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