ReviewBiology methods & protocols2026
Novel reference method for precise determination of tryptophanase activity.
Review in Biology methods & protocols, 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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Who cites it
1 citing paper in PubMed.
- A novel WST-8-based colorimetric method for sensitive and interference-free determination of glutathione peroxidase activity.Biology methods & protocols · 2026Article
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6 authors.
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Abstract
Tryptophanase (TnaA; EC 4.1.99.1) is a pyridoxal 5'-phosphate-dependent enzyme that catalyzes the β-elimination of L-tryptophan into indole, pyruvate, and ammonia. It plays a key role in bacterial signaling and biofilm formation and is industrially relevant for L-tryptophan biosynthesis. Existing assay methods for TnaA activity measurement, including Kovács reagent colorimetry, HPLC, and NADH-coupled spectrophotometry, each carry limitations in cost, complexity, or analytical sensitivity that restrict their routine use. The current study aims to develop and validate a simple, cost-effective spectrophotometric method for quantifying TnaA activity using 2,4-dinitrophenylhydrazine (2,4-DNPH) as a chromogenic reagent, targeting the pyruvate product of the enzymatic reaction. The DNPH-TnaA assay uses a stable hydrazone complex formed between pyruvate and 2,4-DNPH, which is measurable at 432 nm. It was applied to
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