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Evidence-Based Complementary and Alternative Medicine
Volume 2015 (2015), Article ID 309214, 6 pages
http://dx.doi.org/10.1155/2015/309214
Research Article

Purification and Characterization of Asparaginase from Phaseolus vulgaris Seeds

1Biochemistry Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia
2Biology Department, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia

Received 29 May 2015; Accepted 19 August 2015

Academic Editor: Roberto Miniero

Copyright © 2015 Saleh A. Mohamed et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

L-asparaginase from bacteria has been used in treatment of acute lymphoblastic leukemia. The aim of this study was to purify and characterize L-asparaginase from Phaseolus vulgaris seeds instead of microbial sources. L-asparaginase was purified to apparent homogeneity. The enzyme has molecular mass of 79 kDa. The purified asparaginase had very low activity toward a number of asparagine and glutamine analogues. L-asparaginase was free from glutaminase activity. Kinetic parameters, Km and Vmax of purified enzyme, were found to be 6.72 mM and 0.16 μM, respectively. The enzyme had optimum pH at 8.0. The enzyme showed high stability at alkaline pH (pH 7.5–9.0) when incubated for up to 24 h. L-asparaginase had the same temperature optimum and thermal stability at 37°C. K+ was able to greatly enhance the activity of asparaginase by 150% compared with other metals tested. In conclusion, L-asparaginase showed no glutaminase activity and good stability over a wide range of physiological conditions, and thus it could be used as a potential candidate for treatment of acute lymphoblastic leukemia.