Characterization of a New L-Glutaminase Produced by Achromobacter xylosoxidans RSHG1, Isolated from an Expired Hydrolyzed L-Glutamine Sample

Saleem, Rabia; Ahmed, Safia

doi:10.3390/catal11111262

Cited by 7 publications

(3 citation statements)

References 49 publications

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“…Glutaminase enzyme activity was enhanced by a number of metal ions, such as sodium chloride and thus can be used in food industry. 50 These studies show the importance of marine filamentous fungi in production of glutaminase enzyme. Several bacteria also were shown to produce Glutaminase enzyme.…”

Section: Discussionmentioning

confidence: 90%

Bioprospecting of Marine Fungi from Coastal Karnataka Region as Potential Source of Economically Important Enzyme L-Glutaminase and their Comparative Genomic Study

Rao¹,

Sadananda²,

Pakkala³

et al. 2023

J. Pure Appl. Microbiol.

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Marine fungi are important sources of new metabolites including certain enzymes of medical interest due to their enormous capacity to adapt themselves to extreme environments. Living in a highly competitive ecological niche, they produce certain unusual chemical moieties. Marine biological resources are green, abundant, renewable and aid in economic development. The present study investigates the production of L-Glutaminase which is of therapeutic and industrial importance, from marine fungi of coastal Karnataka. Primary screening on agar plates and submerged fermentation in broth was employed for enzyme production. Both marine yeasts (Pichia sp) and filamentous fungal strains (Aspergillus, Penicillium) were found to be efficient producers of L-Glutaminase. Of the 42 isolates, five potential strains were selected through primary screening and Thin Layer Chromatography was performed to confirm the production. Filamentous fungi were identified through morphological and molecular methods as Penicillium and Aspergillus strains with 99-100% similarity. A. foveolatus (MT667385)and A. nidulans (MT667422) were potential producers (1.58U/ml and 1.41IU/ml). The yeast identified was Pichia kudriavzevii (MT667428), which was a moderate producer of Glutaminase and first marine yeast reported for this enzyme production. Neosartorya quadricincta (MT667427) and P. citrinum (MT667426) are also moderate producers. After screening the marine fungi, the isolated strains’ potential to produce L-Glutaminase was confirmed using SDS PAGE, FTIR and Mass analysis. This study emphasizes the necessity of marine fungal culturing and the scope of use of these fungi for further commercial production of L-Glutaminase which would uplift marine economy.

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Section: Discussionmentioning

confidence: 90%

Bioprospecting of Marine Fungi from Coastal Karnataka Region as Potential Source of Economically Important Enzyme L-Glutaminase and their Comparative Genomic Study

Rao¹,

Sadananda²,

Pakkala³

et al. 2023

J. Pure Appl. Microbiol.

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“…). In many investigations, the ideal temperature for max imal glutaminases activity was around 40-50°C(Nandakumar et al, 2003;Ito et al, 2013;Saleem and Ahmed, 2021). The purified enzyme in our investigation was considered to be heat stable in absence of substrate.…”

mentioning

confidence: 94%

A Highly Purified L-Glutaminase From Immobilized Pseudomonas Sp. Ras123 Cultures With Antitumor and Antibacterial Activities

El-Borai¹,

Sayed

Farag³

et al. 2023

J microb biotech food sci

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L-glutaminase (E.C.3.5.2.1) is an antineoplastic enzyme and in the present study, an extracellular L-glutaminase was produced from a marine local strain identified as Pseudomonas sp. RAS123. The enzyme was produced from free cultures and from cultures immobilized on and in different supports. Pseudomonas sp. RAS123 L-glutaminase produced from immobilized cultures was purified to homogeneity. The specific activity of the enzyme reached 698.655 U/mg protein, with Km and Vmax value of 3.2 mg/ml and 2000 U/ml, respectively. A single band with a molecular weight of about 32.0 kDa was produced by the purified enzyme on SDS-PAGE. Further findings indicated that the pure enzyme's maximum activity occurred at 50°C and pH 9. The enzyme was stable at 60°C for 60 min and in the pH range of 8.0 to 10.0, The effect of chemicals showed that Mn2+, Mg2+, Ni2+ and Fe2+activated the enzyme, while SDS (10% w/v) strongly inhibited the activity of the enzyme. The purified enzyme showed cytotoxic activity against HCT-116, HepG2, MCF-7, HeLa, and CCL-86 cell lines tested with IC50 values of 122, 175, 195, 306, and > 500 µg/ml, respectively. Also, the antibacterial effect of the enzyme showed activity against Staphylococcus aureus, Bacillus subtilis, Streptococcus mutants, Enterobacter cloacae and Escherichia coli. These findings demonstrate that L-glutaminase might be used in numerous biotechnological applications, particularly food and pharmaceutical processing.

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“…L-glutamine is a unique molecule classified as a semiessential or conditionally essential amino acid with two nitrogen side chains. The amino acid L-glutamine is used for ammonia and nitrogen transport in the human body [22]. L-ornithine is also an amino acid produced by the separation of urea from L-arginine in the body's urea cycle.…”

Section: Introductionmentioning

confidence: 99%

Synthesis of L-Ornithine- and L-Glutamine-Linked PLGAs as Biodegradable Polymers

Taşkor Önel

2023

Polymers

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L-ornithine and L-glutamine are amino acids used for ammonia and nitrogen transport in the human body. Novel biodegradable synthetic poly(lactic-co-glycolic acid) derivatives were synthesized via conjugation with L-ornithine or L-glutamine, which were selected due to their biological importance. L-ornithine or L-glutamine was integrated into a PLGA polymer with EDC coupling reactions as a structure developer after the synthesis of PLGA via the polycondensation and ring-opening polymerization of lactide and glycolide. The chemical, thermal, and degradation property–structure relationships of PLGA, PLGA-L-ornithine, and PLGA-L-glutamine were identified. The conjugation between PLGA and the amino acid was confirmed through observation of an increase in the number of carbonyl carbons in the range of 170–160 ppm in the 13C NMR spectrum and the signal of the amide carbonyl vibration at about 1698 cm−1 in the FTIR spectrum. The developed PLGA-L-ornithine and PLGA-L-glutamine derivatives were thermally stable and energetic materials. In addition, PLGA-L-ornithine and PLGA-L-glutamine, with their unique hydrophilic properties, had faster degradation times than PLGA in terms of surface-type erosion, which covers their requirements. L-ornithine- and L-glutamine-linked PLGAs are potential candidates for development into biodegradable PLGA-derived biopolymers that can be used as raw materials for biomaterials.

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Characterization of a New L-Glutaminase Produced by Achromobacter xylosoxidans RSHG1, Isolated from an Expired Hydrolyzed L-Glutamine Sample

Cited by 7 publications

References 49 publications

Bioprospecting of Marine Fungi from Coastal Karnataka Region as Potential Source of Economically Important Enzyme L-Glutaminase and their Comparative Genomic Study

Bioprospecting of Marine Fungi from Coastal Karnataka Region as Potential Source of Economically Important Enzyme L-Glutaminase and their Comparative Genomic Study

A Highly Purified L-Glutaminase From Immobilized Pseudomonas Sp. Ras123 Cultures With Antitumor and Antibacterial Activities

Synthesis of L-Ornithine- and L-Glutamine-Linked PLGAs as Biodegradable Polymers

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