African Journal of
Agricultural Research

  • Abbreviation: Afr. J. Agric. Res.
  • Language: English
  • ISSN: 1991-637X
  • DOI: 10.5897/AJAR
  • Start Year: 2006
  • Published Articles: 6666

Full Length Research Paper

Some biochemical properties of catalase from safflower (Carthamus tinctorius L. cv. M-CC-190)

H. Tayefi-Nasrabadi1*, G. Dehghan2, B. Daeihassani2, A. Movafegi2 and A. Samadi3
  1Department of Biochemistry, Faculty of Veterinary Medicine, University of Tabriz, Tabriz, Iran. 2Department of Plant Sciences, Faculty of Natural Sciences, University of Tabriz, Tabriz, Iran. 3Department of Soil Sciences, Faculty of Agriculture, Urmia University, Urmia, Iran.
Email: [email protected], [email protected]

  •  Accepted: 08 April 2011
  •  Published: 19 October 2011

Abstract

 

Safflower (Carthamus tinctorius L.cv) is a member of the family Compositae that is cultivated mainly for its seed, which is used as edible oil and bird seed. Catalase is a common enzyme found in nearly all living organisms that are exposed to oxygen, where it functions to catalyse the decomposition of hydrogen peroxide to water and oxygen. In this study catalase was extracted from leaves of safflower (cv. M-CC-190) using phosphate buffer (0.1 M, pH 7.2) and its kinetic properties, thermal stability, isozymic pattern and sensitivity to inhibitors were investigated. On the basis of pH profile and activity staining for catalase on native PAGE, two isoform of catalases were detected in extract with pH optima at 6.5 and 8.5, and the range of catalase activity was found between 5.5 and 10.5. Apparent Km and Vmax of catalase at two pH optima were different, but the catalytic efficiency values were similar. Effect of heat treatment on catalase activity showed lower heat stability for isoenzyme active at pH 8.5. Isoenzyme with pH optima at 6.5 was more sensitive to both azide and cyanide in comparison to other isoenzyme active in M-CC-190 leaves extract.

 

Key words: Catalase, safflower, isoenzyme, kinetic, thermal stability, M-CC-190.