Abstract
As significant biocatalyst, L-glutaminases find potential applications in various fields, from nourishment to the pharmaceutical industry. Anticancer activity and flavor enhancement are the most promising applications of L-glutaminases. In this study, L-glutaminase was isolated and purified from an old glutamine sample. A selected bacterial isolate was characterized taxonomically by morphological characters, biochemical testing and 16S rDNA sequence homology testing. The taxonomical characterization of the isolate identified it as Achromobacter xylosoxidans strain RSHG1. The isolate showed maximum enzyme production at 30 °C, pH 9, with Sorbitol as a carbon source and L-Glutamine as a nitrogen and inducer source. L-Glutaminsae was purified by using column chromatography on a Sephadex G-75. The enzyme has a molecular weight of 40 KDa, pH optimal 7 and is stable in the pH range of 6–8. The optimum temperature for the catalyst was 40 °C and stable at 35–50 °C. The kinetic studies of the purified L-glutaminase exhibited Km and Vmax of 0.236 mM and 443.8 U/mg, respectively. L-Glutaminase activity was increased when incubated with 20 mM CaCl2, BaCl2, ZnSO4, KCl, MgSO4 and NaCl, whereas EDTA, CoCl2, HgCl, ZnSO4 and FeSO4 decreased the activity of the enzyme. The addition of 8% NaCl enhanced the glutaminase activity. L-Glutaminase immobilized on 3.6% agar was stable for up to 3 weeks.
Highlights
Biocatalysts play a crucial role in maintaining and sustaining the food, chemical, agriculture and cosmetic industries as commercially economic products
The present study shows the isolation, characterization and identification of bacterial isolates with optimization of L-glutaminase by selected bacterial strains isolated from old glutamine samples
The bacterial strain RSHG1 was selected based on secondary screening performed by point inoculation of the bacterial strain on glutamine salt medium
Summary
Biocatalysts play a crucial role in maintaining and sustaining the food, chemical, agriculture and cosmetic industries as commercially economic products. Enzymatic processes are eco-friendly, which reduces the risk of byproducts that are toxic for the human health and the environment [4] Due to these features, biocatalysts play a vital role in the pharmaceutical industry [2]. L-Glutaminases are amidohydrolases, belong to the hydrolase class of enzymes and cleave L-glutamine into L-glutamic acid and ammonia This enzyme plays a significant role in nitrogen metabolism at the cellular level. Due to the importance of this enzyme, the aim of the present research study is to isolate new indigenous bacterial strains with higher levels of L-glutaminase production, with high pH stability and salt tolerance that can be used in the food industry and as biosensors in the pharmaceutical industry
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