ArticleMicrobial cell factories2025
Biochemical and biological evaluation of L-glutaminase from Aspergillus tamarii AUMC 10198 via solid-state fermentation.
Article in Microbial cell factories, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed.
- L-asparaginase by filamentous fungi and yeasts from lichens and soils across maritime Antarctic islands.Extremophiles : life under extreme conditions · 2026Article
- Untapped microbial factories for next-generation therapeutics: Endophytic fungi of medicinal plants.Microbial cell factories · 2026Review
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4 authors.
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Abstract
introductionFungal L-glutaminase has recently attracted growing interest due to its potential applications in medical therapy and biotechnology. This study aimed to develop a cost-effective bioprocess for L-glutaminase production using agricultural by-products under solid-state fermentation (SSF). Several fungal isolates were screened for extracellular L-glutaminase production, and the native isolated strain Aspergillus tamarii AUMC 10198 was identified as a potent high-yield producer. Process parameters influencing enzyme production were systematically optimized using a one-variable-at-a-time (OVAT) approach. The enzyme was subsequently purified through a three-step procedure and characterized for its biochemical properties. Notably, the purified L-glutaminase also exhibited antimicrobial activity, suggesting potential therapeutic applications.
resultsThe native fungus Aspergillus tamarii AUMC 10198, registered under GenBank accession number OQ976977, was identified as a potent producer of L-glutaminase under solid-state fermentation (SSF) using wheat bran as the solid substrate. The solid-state yield of L-glutaminase exhibited a 3.20-fold increase in comparison to the unoptimized state. L-glutaminase produced by Aspergillus tamarii AUMC 10198 was purified through three successive steps, leading to a 12.90-fold enhancement in enzyme activity. As a result of the purification process, the final enzyme recovery was 18.45%. The isolated L-glutaminase exhibited optimal activity at a pH of 8, a temperature of 45 °C, and partial stability up to 60 °C, as determined by characterization. The purified L-glutaminase exhibited a Vmax of 10.10 U/ml and a km of 0.28 mg/ml when glutamine was used as the substrate. The metal ions Fe
conclusionThis study highlights the remarkable properties of L-glutaminase produced by the native potent fungal isolate Aspergillus tamarii AUMC 10198, underscoring its significant potential for industrial applications and pharmaceutical drug development.
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