期刊名称：American Journal of Food Science and Technology
印刷版ISSN：2333-4827
电子版ISSN：2333-4835
出版年度：2013
卷号：1
期号：3
页码：30-35
DOI：10.12691/ajfst-1-3-4
语种：English
出版社：Science and Education Publishing
摘要：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 Km 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.
