L-ASPARAGINASE AND L-GLUTAMINASE FROM Pseudomonas aeruginosa PAO1: PRODUCTION AND SOME PHYSICOCHEMICAL PROPERTIES

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October – November 2015, vol. 5, no. 2
pages: 142-146
Article type: Microbiology of Microbiology
DOI: 10.15414/jmbfs.2015.5.2.142-146
Abstract: L- asparaginase (EC 3.5.1.1) is an enzyme which converts L- asparagine to L-aspartic acid and ammonia; L- glutaminase (EC 3.5.1.2) is an enzyme which catalyzes the conversion of L-glutamine to L- glutamic acid and ammonia. Both of these enzymes have been used in as chemotherapeutic agents. Among different sources of L- asparaginase and L-glutaminase enzymes producers, microbial strains possess an elevated edge over other enzyme producers; these enzymes produced by different microbial strains differ in some physiological, biochemical, catalytic and immunological properties. This led to the continuous screening program for isolation of novel microbial strains that could produce an effective enzyme with few limitations at use. A bacterial strain isolated from soil and identified as Pseudomonas aeruginosa PAO1 had been found to be capable of producing both extracellular L- Asparaginase and L- Glutaminase enzymes. The enzymes were produced under solid state fermentation. Effects of different fermentation parameters for production of these enzymes were determined. Some physicochemical properties of both of these enzymes were determined. The results obtained in this study revealed the potential of Pseudomonas aeruginosa PAO1 as a source of both L-Asparaginase and L- Glutaminase enzymes, which have gained significance in pharmaceutical industry. The uses of inexpensive agro- industrial wastes in this study have important economic advantages over submerged fermentation.
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