Production, characterization, and applications of a novel thermo-acidophilic L-asparaginase of Pseudomonas aeruginosa CSPS4

Abstract

In present investigation, a potential L-asparaginase-producing bacterial isolate, Pseudomonas aeruginosa CSPS4, has been explored to enhance the production and purification of the asparaginase enzyme. Production of L-asparaginase is enhanced using the 'one variable at a time approach (OVAT)'. In Placket Burman (PB) analysis, pH, sucrose, and temperature significantly influence L-asparaginase production. Thereafter, L-asparaginase enzyme was recovered from culture broth using fractional precipitation with chilled acetone. The partially purified L-asparaginase showed a molecular weight of ~35 KDa on SDS-PAGE. L-asparaginase was characterized as a thermo-acidophilic enzyme exhibiting optimum pH and temperature of 6.0 and 60 °C, respectively. These characteristics render this enzyme novel from other available asparaginases of Pseudomonas spp. L-asparaginase activity remained unaffected by different modulators. L-asparaginase of this investigation was successfully employed for acrylamide degradation in commercial fried potato chips, establishing its applicability in food industries.