Characterization of l-asparaginase purified from pole

Abstract EN

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.