J Bio Life Sci 2011 2(1):11-15
Journal of Biology & Life Sciences
Partial Purification and Some Properties of Catalase from Dill (Anethum graveolens L.)
Sakarya University, Faculty of Arts & Science, Department ofChemistry, 54187 Sakarya, Turkey Received: 04.11.2010 Accepted: 04.12.2010 Published: 26.12.2010
Abstract Catalase (CAT: EC 184.108.40.206) is a metalloenzyme which dismutes hydrogen peroxide to water and oxygen. It is widely distributed in animals, plants, all aerobic microorganisms. Most of work performed on this enzyme obtained from mammalian, bacteria and fungal sources as there is less work about plant catalases. In this work, partial purification of catalase from dill (Anethum graveolens L.) and the kinetic properties were investigated. For the purification, enzyme was extracted from dill with phosphate buffer and centrifuged. Then (NH4)2SO4 precipitation was performed to the extracted enzyme and was dialyzed. After dialysis, the extract was loaded and eluted from a sephadex G200 column with phosphate buffer. The overall partial purification was about 5.5-fold. A temperature of 4°C was maintained during the purification process. Enzyme activity was spectrophotometrically measured at 240 nm. The optimal pH and temperature were determined as 7.0 and 30°C. In addition, KM and Vmax values were determined with H2O2 by means of Lineweaver-Burk plots. KM and Vmax of dill catalase was 24.0 mM and 3333.33 U/mL respectively. The effect of citric acid, KCN, NaN3, NaCl and CuSO4 on dill catalase activity was investigated and the results showed that KCN and NaN3 had good inhibitory effect.
Key words: Purification, Catalase, Dill, Properties
Corresponding Author: G.Arabaci, e-mail: email@example.com, Phone: +902642956048, Fax:+ 902642955950
INTRODUCTION Catalase (CAT, H2O2:H2O2 oxidoreductase; EC 220.127.116.11) by scavenging hydrogen peroxide to water and oxygen is an important enzyme of...