Future University In Egypt (FUE)
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Nada Anwar AbdelRazek

Basic information

Name : Nada Anwar AbdelRazek
Title: Assistant Lecturer
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Personal Info: Nada Anwar, Master degree, Assistant Lecturer in Microbiology and Immunology department; Bsc in pharmacy, Ain shams university.Currently working on her Master Degree at microbiology and immunology department faculty of pharmacy Ain Sams Uiveristy. View More...


Certificate Major University Year
Masters Micro baiolgy Ain Shams University - Faculty of Pharmacy 2018
Bachelor Faculty Of Pharmaceutical Sciences Ain Shams University - Facualty Of Pharmacy 2009

Teaching Experience

Name of Organization Position From Date To Date
NODCAR (National Organization for Drug Control & Research) Microbiologist 03/08/2010 28/08/2012

Researches /Publications

Diverse origins of microbial L-asparaginases and their current miscellaneous applications - 01/0

Nada Anwar Abdelrazek Hegazy

Walid Faisal Elkhatib, Mohammad Aboulwafa


L-asparaginase, also known as amidohydrolase, catalyzes the breakdown of asparagine into aspartic acid and ammonia. Due to its ability to inhibit the biosynthesis of protein lymphoblasts, it is used to treat acute lymphoblastic leukemia (ALL). It also has other applications in the food industry by preventing the formation of acrylamide. Different organisms including bacteria, fungi, actinomycetes, and plants produce L-asparaginase. This review highlights different applications of L-asparaginase in the industrial fields, the major sources of L-asparaginase, its immunological reactions and production techniques through the solid state (SSF) and submerged (SmF) fermentation as well as optimization of the production process.

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Experimental and bioinformatics study for production of l-asparaginase from Bacillus licheniformis: a promising enzyme for medical application - 01/0

Nada Anwar Abdelrazek Hegazy

Walid F. Elkhatib, Mohammad M. Aboulwafa


A Bacillus licheniformis isolate with high L-asparaginase productivity was recovered upon screening two hundred soil samples. This isolate produces the two types of bacterial L-asparaginases, the intracellular type I and the extracellular type II. The catalytic activity of type II enzyme was much higher than that of type I and reached about 5.5 IU/ml/h. Bioinformatics analysis revealed that L-asparaginases of Bacillus licheniformis is clustered with those of Bacillus subtilis, Bacillus haloterans, Bacillus mojavensis and Bacillus tequilensis while it exhibits distant relatedness to L-asparaginases of other Bacillus subtilis species as well as to those of Bacillus amyloliquefaciens and Bacillus velezensis species. Upon comparison of Bacillus licheniformis L-asparaginase to those of the two FDA approved L-asparaginases of E. coli (marketed as Elspar) and Erwinia chrysanthemi (marketed as Erwinaze), it observed in a cluster distinct from- and with validly predicted antigenic regions number comparable to those of the two mentioned reference strains. It exhibited maximum activity at 40 °C, pH 8.6, 40 mM asparagine, 10 mM zinc sulphate and could withstand 500 mM NaCl and retain 70% of its activity at 70 °C for 30 min exposure time. Isolate enzyme productivity was improved by gamma irradiation and optimized by RSM experimental design (Box–Behnken central composite design). The optimum conditions for maximum L-asparaginase production by the improved mutant were 39.57 °C, 7.39 pH, 20.74 h, 196.40 rpm, 0.5% glucose, 0.1% ammonium chloride, and 10 mM magnesium sulphate. Taken together, Bacillus licheniformis L-asparaginase can be considered as a promising candidate for clinical application as antileukemic agent

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