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Abstract
Isolation and Purification of High Efficiency L-asparaginase by Quantitative Preparative Continuous-elution SDS PAGE Electrophoresis
An Unique extracelluar glutaminase free L-asparaginase from novel marine Actinomycetes was isolated to perceptible homogeneity in agro industrial wastes. Quantitative Preparative Continuous-Elution SDS PAGE Electrophoresis is a high-resolution method for the preparative isolation of L-Asparaginase in biological samples. The enzyme was purified 248.68-fold and showed a final specific activity of 5035.28 IU/mg with an 80.71% yield. The homotetramer enzyme has a molecular mass of 133.25 kDa and an isoelectric point of approximately 5.4.Kinetic parameters, Km and Vmax of purified L-asparaginase from Streptomyces radiopugnans MS1 were found to be 0.0598, 3.5478 IU μg - 1 respectively. The de novo sequencing strategy presented here provides a rapid and reliable means to identify proteins in Streptomyces radiopugnans MS1. The purified L-asparaginase has no glutaminase activity, which can diminish the leeway of side effects during the itinerary of anti-malignancy therapy.