Purification of Catalase by Modified Procedure and some Properties of Enzyme

Nguyen Hoang An, Godagama Gamarchchige Dinesh Suminda, Nguyen Thi Thu Phuong, Dinh Nho Thai, Nguyen Thi Hong Loan


Catalase (EC plays an important role in protecting organism from oxidative effect by breaking down H2O2 into H2O and O2 molecules. In this study, a modified procedure for catalase from bovine liver and its properties were reported. Bovine liver catalase was purified to electrophoretic homogeneity as a single protein band around 60 kDa on SDS-PAGE by acetone fractionation, followed by ion-exchange chromatography on DEAE-Sepharose and CM-Sepharose columns. The specific activity of the purified catalase was 79,277 units per mg of protein (U/mg) with 1.87% recovery and purification fold was roughly 60 times. The catalase was a homo-tetramer with a molecular mass of about 240.987 kDa as determined by native gel electrophoresis. The purified enzyme showed the highest activity at pH 7, 37°C, and remained active over a broad range of pH from 5 to 10 and range of temperature from 4°C to 40°C. Its activity was inactivated by incubating in 60°C for 30 min. The activity of the enzyme was induced by Ca2+ and inhibited by Na+, Ni2+, Cu2+, Zn2+, Fe2+, Fe3+ and NaN3. Under the optimal conditions, Km and Kcat/Km values of the catalasewas found to be 23,69 mM and Kcat/Km = 5.106 (M.s)-1, respectively


Bovine liver catalase, purification, oxidative effect.

Full Text:


DOI: https://doi.org/10.15625/0866-7160/v40n2.10893 Display counter: Abstract : 178 views. PDF : 155 views.


          mitra usaha tani       budidayatani.com

Editorial Office:

1st Floor, A16 Building, 18B Hoang Quoc Viet Street, Cau Giay District, Hanoi, Vietnam

Tel: (+84) 24 3791 7101

Email: tapchisinhhoc@vjs.ac.vn