International Journal of Research & Review (www.ijrrjournal.com) 177 Vol.5; Issue: 8; August 2018 International Journal of Research and Review www.ijrrjournal.com E-ISSN: 2349-9788; P-ISSN: 2454-2237 Original Research Article Production, Partial Purification and Assay of L- Glutaminase Enzyme from Aspergillus Niger by Solid State Fermentation Nagamani J.E Garden City University, School of Sciences, Bangalore-560 049, Karnataka, India ABSTRACT L-Glutaminase (L-Glutamine amidohydrolase, EC 3.5.1.2) is the important enzyme that catalyzes the deamination of L-Glutamine to L-glutamic acid and ammonium ions. Of late L-Glutaminase has received much attention with respect to its therapeutic and industrial applications. It acts as a potent antileukemic agent and has flavor enhancing property for fermented foods. Glutaminase production is widely distributed in plants, animals, bacteria, yeasts, and fungi. This study investigates the production and partial purification of extracellular Glutaminase enzyme from Aspergillus niger using agricultural waste by solid state fermentation (SSF). 80% ammonium sulphate fractionated enzyme exhibited maximum activity of 10.932μM/ml/min and a specific activity of 0.879U/mg protein. Keywords: L-Glutaminase, Aspergillus niger, SSF, Activity, Specific activity INTRODUCTION L-Glutaminase (L-Glutamine amidohydrolase EC 3.5.1.2.) is the enzyme deamidating L-Glutamine to L-Glutamic acid and ammonia. Glutaminase is ubiquitous in microorganisms and it plays a major role in the cellular metabolism of both prokaryotes and eukaryotes. In general, Glutaminases from Escherichia coli, Pseudomonas spp., Rhizobium etli, Micrococcus luteus K-3, Bacillus spp., Clostridium welchii, Vibrio costicola, Zygosaccharomyces rouxii and Aspergillus oryzae have been isolated and well studied. L-Glutamine is used as obligate nitrogen donor for the biosynthesis of purine and pyrimidine nucleotides in a living cell. Tumor cells have no mechanism to synthesize L-Glutamine and hence take it as an exogenous source. L- Glutaminase causes selective death of glutamine- dependent tumor cells by depriving cells with L-Glutamine, and hence it is used as an effective agent in the treatment of acute lymphocytic leukemia and HIV. [1] In food industry, L-Glutaminase is used as a flavour enhancer by increasing glutamic acid content in food through hydrolysis of L-Glutamine to L-Glutamic acid and ammonia. Since the sources for L- Glutaminase are limited, the search for potential microbial strains that produce the enzyme with novel properties for their industrial production is being pursued all over the world. [2] Glutaminase is also taking an important role that controls the delicious taste of fermented foods such as soy sauce and in general food products by increasing the glutamic acid content therefore, this enzyme has attracted a great attention in food industries. [3] Its commercial importance demands the search for new and better yielding microbial strains and economically viable bioprocesses for its large-scale production. [4] Different methods of fermentation technology can be applied for the production of L-Glutaminase. Commercial production of L-Glutaminase had been carried out using submerged fermentation