ArticleApplied microbiology and biotechnology2026
Immobilization of TtAlaDH on magnetic nanoparticles: effects on stability and reuse.
Article in Applied microbiology and biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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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1 citing paper in PubMed.
- Immobilized Wild-Type and Mutant L‑Alanine Dehydrogenase fromACS omega · 2026Article
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4 authors.
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Abstract
L-Alanine dehydrogenase (L-AlaDH) is a microbial enzyme that catalyzes the reversible oxidative deamination of L-Alanine to pyruvate. This enzyme catalyzes the reversible conversion of L-Alanine to pyruvate, while concurrently maintaining redox homeostasis through the NAD + /NADH coenzyme system. Despite the critical role of the L-AlaDH enzyme in biotechnological amino acid production, its implementation is hampered by poor operational stability, specifically difficulties in maintaining activity at high temperatures and ensuring adequate reusability. In this study, the recombinant plasmid encoding TtAlaDH from Thermus thermophilus was transformed into E. coli BL21 (DE3) for heterologous expression and was successfully immobilized on the surface of functionalized magnetic nanoparticles (F-NH
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