Evidence for Peroxidase Activity in Caralluma umbellata
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  • 作者:Raghu Ram Achar (1) (2)
    B. K. Venkatesh (1) (2)
    P. Sharanappa (3)
    B. S. Priya (4)
    S. Nanjunda Swamy (1)
  • 关键词:Caralluma umbellata Peroxidase ; CUP ; L ; AAO
  • 刊名:Applied Biochemistry and Biotechnology
  • 出版年:2014
  • 出版时间:August 2014
  • 年:2014
  • 卷:173
  • 期:8
  • 页码:1955-1962
  • 全文大小:524 KB
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  • 作者单位:Raghu Ram Achar (1) (2)
    B. K. Venkatesh (1) (2)
    P. Sharanappa (3)
    B. S. Priya (4)
    S. Nanjunda Swamy (1)

    1. Department of Biotechnology, JSS Technical Institutions Campus, Mysore, Sri Jayachamarajendra College of Engineering, Karnataka, 570 006, India
    2. JSS Research Foundation, JSS Technical Institutions Campus, Mysore, Karnataka, 570 006, India
    3. Department of Studies in Biosciences, University of Mysore, Hemagangothri, Hassan, Karnataka, 570 006, India
    4. Department of Studies in Chemistry, University of Mysore, Manasagangothri, Mysore, Karnataka, 570 006, India
  • ISSN:1559-0291
文摘
Vast applications of peroxidases create an increasing demand to characterize peroxidases from new sources with more applicability potential. The aim of the present study was to check the presence of peroxidase activity from Caralluma umbellata. This is the first report on the C. umbellata peroxidase (CUP). The presence of peroxidase was revealed by the histochemical analysis of the stem sections, zymographic studies, and in vitro peroxidase activity assay using various reducing substrates viz., 2, 2-azinobis (3-ethylbenzthiazoline-6-sulfonic acid) (ABTS), guaiacol, o-dianisidine, and ferulic acid. The band pattern in zymogram confirms that CUP has a molecular weight less than that of horseradish peroxidase (44?kDa). Comparative evaluation of peroxidase activity of CUP with respect to horseradish peroxidase (HRP) indicates that CUP catalyzes ABTS and ferulic acid in a similar pattern as HRP but with guaiacol, the extent of catalysis shown by CUP over HRP is high. The standard inhibitors sodium azide and sodium meta bisulphite inhibited CUP activity in a dose dependent manner.

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