Recent advances in microbial glutaminase production and applications—a concise review

Amobonye, Ayodeji; Singh, Suren

doi:10.1080/07388551.2019.1640659

Cited by 40 publications

(19 citation statements)

References 110 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…There are two isoenzymes in mammalian cells (Gls1 and Gls2) encoded by two distinct genes: GLS1 and GLS2, respectively [168]. Normally, these proteins are located in the inner membrane of the mitochondria and primarily expressed in the brain, liver, and kidney, which play an essential metabolic role in generating energy, synthesizing the neurotransmitter glutamate, and maintaining acid-base equilibrium in the kidney [169,170]. The upregulation of Gls1 has been reported in cancer cells to support tumor cell growth [171,172].…”

Section: Glutaminasementioning

confidence: 99%

The Non-canonical Role of Metabolic Enzymes in Immune Cells and Its Impact on Diseases

Alves

Doretto-Silva

Silva

et al. 2020

Curr. Tissue Microenviron. Rep.

View full text Add to dashboard Cite

Section: Glutaminasementioning

confidence: 99%

The Non-canonical Role of Metabolic Enzymes in Immune Cells and Its Impact on Diseases

Alves

Doretto-Silva

Silva

et al. 2020

Curr. Tissue Microenviron. Rep.

View full text Add to dashboard Cite

“…L-glutaminase from Pseudomonas 7A has antiviral activity against retroviral disease by disruption in mRNA translation and repression of the viral replication [8]. Also, L-glutaminase from Bacillus amyloliquefaciens has been used as a flavor enhancer in foods [9], while the enzyme from Bacillus cereus LC13 showed antioxidant activity with ascorbic acid [10]. A biosensor for monitoring the L-glutamine in pharmaceutical powders was progressed by immobilizing L-glutaminase from Hypocria jecorina onto nanorods of zinc oxide and chitosan [11].…”

Section: Introductionmentioning

confidence: 99%

“…The exploration of distinct microbial resources with unique properties as well as the enhancement of the bioprocesses using cheap resources and kinetic parameters of purified L-glutaminase are still under development for productivity, therapeutic potential, and industrial issues [19]. The economic challenge of L-glutaminase production required the exploration of new microbial sources with high yield and large-scale production using the available cheap resources [10]. The physical and nutritional factors play a vital role in the submerged fermentation of L-glutaminase production where it depends on the presence of the appropriate substrate and feedback inhibition by the end product [20].…”

Section: Introductionmentioning

confidence: 99%

L-Glutaminase Synthesis by Marine Halomonas meridiana Isolated from the Red Sea and Its Efficiency against Colorectal Cancer Cell Lines

et al. 2021

View full text Add to dashboard Cite

L-glutaminase is an important anticancer agent that is used extensively worldwide by depriving cancer cells of L-glutamine. The marine bacterium, Halomonas meridian was isolated from the Red Sea and selected as the more active L-glutaminase-producing bacteria. L-glutaminase fermentation was optimized at 36 h, pH 8.0, 37 °C, and 3.0% NaCl, using glucose at 1.5% and soybean meal at 2%. The purified enzyme showed a specific activity of 36.08 U/mg, and the molecular weight was found to be 57 kDa by the SDS-PAGE analysis. The enzyme was highly active at pH 8.0 and 37 °C. The kinetics’ parameters of Km and Vmax were 12.2 × 10−6 M and 121.95 μmol/mL/min, respectively, which reflects a higher affinity for its substrate. The anticancer efficiency of the enzyme showed significant toxic activity toward colorectal adenocarcinoma cells; LS 174 T (IC50 7.0 μg/mL) and HCT 116 (IC50 13.2 μg/mL). A higher incidence of cell death was observed with early apoptosis in HCT 116 than in LS 174 T, whereas late apoptosis was observed in LS 174 T more than in HCT 116. Also, the L-glutaminase induction nuclear fragmentation in HCT 116 was more than that in the LS 174T cells. This is the first report on Halomonas meridiana as an L-glutaminase producer that is used as an anti-colorectal cancer agent.

show abstract

“…Numerous bacteria are involved in synthesis of extracellular and intracellular glutaminases such as Bacillus sp., Pseudomonas, Actinobacterium sp, and E. coli. [4].…”

Section: Introductionmentioning

confidence: 99%

Isolation and Characterization of L-Glutaminase producing Bacteria

Saleem

Ahmed

2020

Preprint

View full text Add to dashboard Cite

Being a significant protein L-glutaminases discovers potential applications in various divisions running from nourishment industry to restorative and cure. It is generally disseminated in microbes, actinomycetes, yeast and organisms. Glutaminase is the principal enzyme that changes glutamine to glutamate. The samples were gathered from soil of Taxila, Wah Cantt and Quetta, Pakistan for the isolation of glutaminase producing bacteria. After primary screening, subordinate screening was done which includes multiple testification such as purification, observation of morphological characters and biochemical testing of bacterial strains along with 16S rRNA sequence homology testing. Five bacterial strains were selected showing glutaminase positive test in screening, enzyme production via fermentation and enzymatic and protein assays. Taxonomical characterization of the isolates identified them as Bacillus subtilis U1, Achromobacter xylosoxidans G1, Bacillus subtilis Q2, Stenotrophomonas maltophilia U3 and Alcaligenes faecalis S3. The optimization of different effectors such as incubation time, inducers, carbon source, pH, and nitrogen source were also put under consideration. There was slight difference among incubation of bacterial culture, overall, 36 hours of incubation time was the best for glutaminase production by all the strains. Optimal pH was around 9 in Achromobacter xylosoxidans G1 and Alcaligenes faecalis S3, pH 6 in Bacillus subtilis U1, pH 8 in Stenotrophomonas maltophilia U3, pH 6-8 in Bacillus subtilis Q2. Best glutaminase production was obtained at 37°C by Bacillus subtilis U1and Bacillus subtilis Q2, 30°C for Achromobacter xylosoxidans G1, Stenotrophomonas maltophilia U3 and 25°C by Alcaligenes faecalis S3. The carbon sources put fluctuated effects on activity of enzyme in such a way that glucose was the best carbon source for Bacillus subtilis U1and Bacillus subtilis Q2, Sorbitol for Achromobacter xylosoxidans G1 and Alcaligenes faecalis S3 while xylose was the best for Stenotrophomonas maltophilia U3. Yeast extract and Trypton were among good nitrogen sources for Achromobacter xylosoxidans G1 and of Bacillus subtilis U1 respectively. Glutamine was the best inducer for Bacillus subtilis Q2, Alcaligenes faecalis S3 and Stenotrophomonas maltophilia U3, while lysine for Achromobacter xylosoxidans G1 and glycine act as good inducer in case of Bacillus subtilis U1. After implementation of optimal conditions microbial L-glutaminase production can be achieved and the bacterial isolates have a great potential for production of glutaminase enzyme and their applications.

show abstract

Recent advances in microbial glutaminase production and applications—a concise review

Cited by 40 publications

References 110 publications

The Non-canonical Role of Metabolic Enzymes in Immune Cells and Its Impact on Diseases

The Non-canonical Role of Metabolic Enzymes in Immune Cells and Its Impact on Diseases

L-Glutaminase Synthesis by Marine Halomonas meridiana Isolated from the Red Sea and Its Efficiency against Colorectal Cancer Cell Lines

Isolation and Characterization of L-Glutaminase producing Bacteria

Contact Info

Product

Resources

About