Evidence map›Paper›PMID 42271439›Full record

ArticleJournal of biological engineering2026

MelC tyrosinase-dependent enzymatic synthesis of functional melanins from phenolic monomers.

Nimya Krishnan, Koijam Monica Devi, Chan-Seo Yeo, Kwon-Young Choi

Abstract read
In one paragraph

Article in Journal of biological engineering, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Nimya KrishnanDepartment of Molecular Science and Technology, Ajou University, Suwon, Gyeonggi-do, Republic of Korea.
Koijam Monica DeviDepartment of Molecular Science and Technology, Ajou University, Suwon, Gyeonggi-do, Republic of Korea.
Chan-Seo YeoDepartment of Molecular Science and Technology, Ajou University, Suwon, Gyeonggi-do, Republic of Korea.
Kwon-Young ChoiDepartment of Molecular Science and Technology, Ajou University, Suwon, Gyeonggi-do, Republic of Korea. kychoi@ajou.ac.kr.

Funding

R&D Program of MOTIE/KEIT RS-2025-09312968
6 · The paper itself

Abstract

Sustainable microbial bioproduction offers a promising route to synthesize high-value melanin biopolymers, yet its scalability is fundamentally limited by the high cost of the L-tyrosine precursor. Here, we aimed to overcome this economic barrier by a highly efficient, engineered microbial platform that utilizes recombinant Escherichia coli expressing MelC tyrosinase to convert diverse, cost-effective noncanonical phenolic monomers into customizable melanin-like biopolymers. Among 13 screened substrates, p-Cresol (PC) and 4-hydroxyphenylacetic acid were the most efficient precursors, yielding 2.40 g/L and 3.92 g/L, respectively. Structural analyses (Ultraviolet-visible spectroscopy, Fourier-transform infrared, Solid-state NMR, MALDI-TOF MS, scanning electron microscopy, Energy-dispersive X-ray spectroscopy, X-ray diffraction, EPR) revealed that these biopolymers possess a native eumelanin-like amorphous architecture while exhibiting partial Dimethyl sulfoxide solubility for improved processability. The synthesized eumelanin-like pigments exhibited high thermal stability (retaining > 37% mass at 800 °C) and strong antioxidant activity, with PC-melanin outperforming conventional eumelanin by twenty-fold. Most importantly, these novel substrates are effluents of industrial and agriculture waste. Thus, this strategy frames a new method for bioremediation. These customizable eumelanin-like pigments hold strong potential for demanding industrial applications, including high-temperature coatings and advanced electronics.

Indexed as

E. coliEumelaninL-tyrosineMelaninPhenolsSubstrates

Identifiers

PMID42271439
PMCPMC13480188

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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.