ReviewBiotechnology notes (Amsterdam, Netherlands)2025
Microbial amidases: Characterization, advances and biotechnological applications.
Review in Biotechnology notes (Amsterdam, Netherlands), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
2 citing papers in PubMed.
- Genomic Characterization and Biotechnological Potential of a Skatole-DegradingCurrent issues in molecular biology · 2026Article
- Evidence for microbial-induced transformation of acrylonitrile-butadiene-styrene (ABS) and styrene-acrylonitrile (SAN) polymer blends by plastic-degrading bacteria.Sustainable microbiology · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The amidases (EC 3.5.1.4) are versatile hydrolase biocatalysts that have been the attention of academia and industries for stereo-selective synthesis and bioremediation. These are categorized based on the amino acid sequence and substrate specificity. Notably, the Signature amidase family is distinguished by a characteristic signature sequence, GGSS(S/G)GS, which encompasses highly conserved Ser-Ser-Lys catalytic residues, and the amidases belonging to this family typically demonstrate a broad substrate spectrum activity. The amidases classified within the nitrilase superfamily possess distinct Glu-Lys-Cys catalytic residues and exhibit activity towards small aliphatic substrates. Recent discoveries have underscored the potential role of amidases in the degradation of toxic amides present in polymers, insecticides, and food products. This expands the horizons for amidase-mediated biodegradation of amide-laden pollutants and fosters sustainable development alongside organic synthesis. The burgeoning global production facilities are expected to drive a heightened demand for this enzyme, attributable to its promising chemo-, regio-, and enantioselective hydrolysis capabilities for a variety of amides. Advances in protein engineering have enhanced the catalytic efficiency, structural stability, and substrate selectivity of amidases. Concurrently, the heterologous expression of amidase genes sourced from thermophiles has facilitated the development of highly stable amidases with significant industrial relevance. Beyond their biotransformation capabilities concerning amides, through amido-hydrolase and acyltransferase activities, recent investigations have illuminated the potential of amidase-mediated degradation of amide-containing pollutants in soil and aquatic environments. This review offers a comprehensive overview of recent advancements pertaining to microbial amidases (EC 3.5.1.4), focusing on aspects such as their distribution, gene mining methodologies, enzyme stability, protein engineering, reusability, and biocatalytic efficacy in organic synthesis and biodegradation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.