CHARACTERIZATION OF L-ASPARAGINASE PURIFIED FROM POLE BEANS | ||
| The Iraqi Journal of Agricultural Science | ||
| Article 1, Volume 47, Issue 7, December 2016, Pages 129-137 | ||
| Authors | ||
| H. N. Al Zobaidy; Kh. A. Shakir; G.M. Strasburg | ||
| Abstract | ||
| The Plant samples of P. vulgaris were collected from a glass-house at Michigan State University (USA) and purified to homoginity by several purification steps. The purified enzyme was found to be a homodimer, with a molecular mass of 79.5 ± 2 KDal as estimated by size exclusion chromatography and SDS-PAGE. The optimum pH for enzyme activity and stability were pH 8.5 and 8 respectively, while the optimum temperature for enzyme activity and stability were 37°C and 30°C respectively. The Km, Vmax and kcat values for the enzyme were 0.294 mM, 1.09 mM/min and 893.8 Sec-1 respectively. This study concluded that beans L-Asparaginase appeared to consist of homodimer subunits with a molecular weight of 40.6 KDal, it is active and stable at basic conditions while it does not endure above 60 C° and loses its activity and stability. It is recommended to studying the amino acid sequence of the L-Asparaginase extracted from beans and alignment with other L-Asparaginases using a protein database for molecular comparison and studying the L-Asparaginase application. | ||
| Keywords | ||
| Asparaginase; Pole beans; Homodimer; Characterization; Phaseolus vulgaris L | ||
|
Statistics Article View: 15 PDF Download: 5 |
||