Evidence map›Paper›PMID 41872847›Full record

ArticleJournal of biological engineering2026

Biosensor-guided directed evolution of aldehyde dehydrogenase for improved adipic acid production from caprolactone.

Haetsal Kim, Soo Young Moon, Joon Young Park, Seung-Ho Baek, Bong Hyun Sung, Jeong Wook Lee, Ju Young Lee, Myung Hyun Noh

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.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

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.

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

8 authors.

Haetsal Kim *Synthetic Biology Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), 125, Gwahak-ro, Yuseong-gu, Daejeon, 34141, South Korea.
Soo Young Moon *Graduate School of Engineering Biology, Korea Advanced Institute of Science and Technology (KAIST), 91, Daehak-Ro, Yuseong-Gu, Daejeon, 34051, South Korea.
Joon Young ParkCenter for Bio-Based Chemistry, Korea Research Institute of Chemical Technology (KRICT), 406-30, Jongga-Ro, Jung-Gu, Ulsan, 44429, South Korea.
Seung-Ho BaekCenter for Bio-Based Chemistry, Korea Research Institute of Chemical Technology (KRICT), 406-30, Jongga-Ro, Jung-Gu, Ulsan, 44429, South Korea.
Bong Hyun SungSynthetic Biology Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), 125, Gwahak-ro, Yuseong-gu, Daejeon, 34141, South Korea.
Jeong Wook LeeSchool of Interdisciplinary Bioscience and Bioengineering, Pohang University of Science and Technology, 77 Cheongam-Ro, Nam-Gu, Pohang, Gyeongbuk, 37673, South Korea. jeongwook@postech.ac.kr.
Ju Young LeeGraduate School of Engineering Biology, Korea Advanced Institute of Science and Technology (KAIST), 91, Daehak-Ro, Yuseong-Gu, Daejeon, 34051, South Korea. juyounglee@kaist.ac.kr.
Myung Hyun NohSynthetic Biology Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), 125, Gwahak-ro, Yuseong-gu, Daejeon, 34141, South Korea. mhnoh@kribb.re.kr.

Funding

Korea Research Institute of Bioscience and Biotechnology KGM1302612Korea Research Institute of Chemical Technology KS2642-10National Research Foundation of Korea RS-2024-00445145National Research Foundation of Korea RS-2024-00453085
6 · The paper itself

Abstract

Biological production of adipic acid, a crucial building block in nylon and polymer manufacturing, from renewable feedstocks has attracted attention as a sustainable alternative to the traditional petrochemical production. The enzymatic conversion of ε-caprolactone into adipic acid via alcohol dehydrogenase (ADH2) and aldehyde dehydrogenase (ALDH) represents a promising route due to its short pathway and high theoretical yield. To optimize this conversion route in Escherichia coli and enhance conversion efficiency, we constructed an adipic acid-responsive biosensor for high-throughput screening. By systematically optimizing the biosensor system, we achieved a 7.15-fold dynamic range. Using this biosensor system, we performed directed evolution of the low-activity ALDH and identified variants with improved conversion performance. The K23Q mutant showed a 2.33-fold increase in adipic acid conversion efficiency and subsequent fed-batch fermentation achieved 30.1 g/L of adipic acid production from ε-caprolactone with 92.7% of theoretical maximum yield. These results demonstrate the potential of biosensor-guided enzyme engineering to enhance catalytic efficiency and support the sustainable biological production of adipic acid.

Indexed as

Adipic acid productionBioplastic degradationBiosensor-assisted evolutionDirected evolutionEnzyme engineeringEscherichia coli

Identifiers

PMID41872847
PMCPMC13130800

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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.