eng Science and Education Publishing American Journal of Food Science and Technology 2013-09-21 1 1 30 35 10.12691/ajfst-1-3-4 AJFST2013134 article Pankaj Kumar Chaurasia 1 Shashi Lata Bharati skschemistry@rediffmail.com 1 Sunil Kumar Singh 1 Rama S.S. Yadav 1 Department of Chemistry, D.D.U. Gorakhpur University, Gorakhpur, Uttar Pradesh, India In this communication, authors have reported the peroxidase enzyme in the juice of Beta vulgaris (beet) and studied its different enzymatic properties. The steady state enzyme kinetics of this peroxidase was studied using two substrates i.e. guaiacol and hydrogen peroxide. The K_m values of this peroxidase for the substrates guaiacol and hydrogen peroxide were 900 and 30 μM, respectively. The pH and temperature optima were 6.0 and 60°C, respectively. The enzyme has maximum stability at pH 6.0. The enzyme was most stable at 45 °C and the activation energy for thermal denaturation of the enzyme was 38.6 kJ/mole/K. Activity of this peroxidase is inhibited completely by sodium azide at the concentration of 16 mM. http://pubs.sciepub.com/ajfst/1/3/4/ajfst-1-3-4.pdf Beta vulgaris peroxidase H₂O₂ guaiacol sodium azide