CHARACTERIZATION OF L-ASPARAGINASE PURIFIED FROM POLE BEANS

N. Al Zobaidy, H.; A. Shakir, Kh.; Strasburg, G.M.

	CHARACTERIZATION OF L-ASPARAGINASE PURIFIED FROM POLE BEANS
The Iraqi Journal of Agricultural Science
Article 1, Volume 47, Issue 7, 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

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