Optimization studies on L-glutaminase production from the new marine Pseudomonas sp. RAS123 isolated from Burullus Lake, Kafr El-Sheikh, Egypt | ||
| Alexandria Journal of Science and Technology | ||
| Articles in Press, Accepted Manuscript, Available Online from 17 November 2025 PDF (1.56 M) | ||
| Document Type: Research article | ||
| DOI: 10.21608/ajst.2025.408518.1081 | ||
| Authors | ||
| Aliaa M. El-Borai* ; Rahma A. Sayed; Samy A. El-Aassar | ||
| Department of Botany and Microbiology, Faculty of Science | ||
| Abstract | ||
| It has been demonstrated that microbial anti-cancer enzymes are efficient and cost-effective cancer therapeutic agents. The current study used statistical methods and one-variable-at-a-time (OVAT) methodology to optimize the production media for maximum L-glutaminase synthesis. Pseudomonas sp. RAS123, which was isolated from Brullus Lake, Kafr El-Sheikh, Egypt, and produced the highest L-glutaminase activity (40.826 U/mL) among the tested isolates, was selectively chosen for more studies. OVAT studies showed that after two days of incubation, the maximum enzyme synthesis was achieved. Moreover, the findings showed that the best pH and inoculum size were 7 and 0.5 mL/50 mL medium, respectively. To produce the maximum L-glutaminase activity, glucose was the most effective carbon source, and L-glutamine was the preferred nitrogen source. Plackett-Burman design (PBD) was utilized to further optimize the fermentation conditions to achieve the maximum production. The findings showed that MgSO₄.7H₂O, NaCl, and CaCl₂ had a detrimental impact on the enzyme, while L-glutamine had the opposite effect. The activity reached 80.364 U/mL, which indicated a 1.59-fold increase in enzyme synthesis. Interactions between factors such as L-glutamine, MgSO₄.7H₂O, and CaCl₂.2H₂O were also investigated by Box-Behnken designs (BBD) factorial experimental designs. Compared to the basal condition, the synthesis of L-glutaminase increased by approximately 2.45 times. The model's accuracy and validity were also confirmed by matching the measured L-glutaminase activity (124.25 U/mL) under ideal conditions with the anticipated one (126.19 U/mL). Key words: Marine enzymes, L-glutaminase, OVAT, Plackett-Burman, Box-Behnken | ||
| Keywords | ||
| Marine enzymes; L- glutaminase; OVAT; Plackett-Burman; Box-Behnken | ||
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