Evidence map›Paper›PMID 42399434›Full record

ArticleApplied microbiology and biotechnology2026

Cysteine-S-conjugate β-lyase: a green catalyst for the production of flavor-active mercaptoketones.

Yi-Chi Huang, Hao-Kai Li, Yu-Lun Lin, Hsi Ho, Tze-Chia Lin, Hong-Ting Victor Lin

Abstract read
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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. 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

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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

6 authors.

Yi-Chi HuangDepartment of Food Science, National Taiwan Ocean University, Keelung, R. O. C., Taiwan.
Hao-Kai LiK. F. Lings Co., Ltd., Taoyuan, R. O. C., Taiwan.
Yu-Lun LinDepartment of Food Science, National Taiwan Ocean University, Keelung, R. O. C., Taiwan.
Hsi HoK. F. Lings Co., Ltd., Taoyuan, R. O. C., Taiwan.
Tze-Chia LinK. F. Lings Co., Ltd., Taoyuan, R. O. C., Taiwan. tzechia.lin@gmail.com.
Hong-Ting Victor LinDepartment of Food Science, National Taiwan Ocean University, Keelung, R. O. C., Taiwan. HL358@ntou.edu.tw.ORCID http://orcid.org/0000-0002-8737-208X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sulfur-containing aroma compounds, which are key determinants of the sensory profile and consumer acceptance of many foods, have received limited research attention regarding the liberation of these thiol aromas via exogenous enzymes. In this study, we characterized and successfully overexpressed an active cysteine-S-conjugate β-lyase (MetC) from the marine bacterium Shewanella putrefaciens, and we also established its optimal catalytic conditions. Kinetic analysis demonstrated effective activity of the enzyme toward natural substrates and aroma mercaptoketone precursors. Size-exclusion chromatography indicated a tetrameric structure for MetC. For most substrates, the apparent catalytic efficiency (

Indexed as

Carbon-Sulfur LyasesCysteineFlavoring AgentsKetonesShewanella putrefaciensSulfhydryl CompoundsKineticsSubstrate SpecificityCarbon-Sulfur LyasesCysteineFlavoring AgentsKetonesSulfhydryl Compounds4-Mercapto-4-methylpentan-2-oneAroma compoundsCysteine-S-conjugate β-lyase (MetC)MercaptoketonesShewanella putrefaciens

Identifiers

PMID42399434
PMCPMC13601414

What OpenQuestion holds

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Registered trials

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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.