Evidence map›Paper›PMID 34764337›Full record

ArticleScientific reports2021

Increased carvone production in Escherichia coli by balancing limonene conversion enzyme expression via targeted quantification concatamer proteome analysis.

Erika Yoshida, Motoki Kojima, Munenori Suzuki, Fumio Matsuda, Kazutaka Shimbo, Akiko Onuki, Yousuke Nishio, Yoshihiro Usuda, Akihiko Kondo, Jun Ishii

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.1field-weighted citation impact, top 22% of its field
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

6 citing papers in PubMed, 19 citations in OpenAlex.

  1. Synthetic and systems biotechnology · 2026
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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

10 authors at 4 institutions in 1 country.

Erika YoshidaGraduate School of Science, Technology and Innovation, Kobe University, 1-1 Rokkodai, Nada, Kobe, 657-8501, Japan. erika.yoshida.ti4@asv.ajinomoto.com.
Motoki KojimaKNC Bio Research Center, KNC Laboratories Co, Ltd. 1-1-1, Murotani, Nishi-ku, Kobe, 651-2241, Japan.
Munenori SuzukiKNC Bio Research Center, KNC Laboratories Co, Ltd. 1-1-1, Murotani, Nishi-ku, Kobe, 651-2241, Japan.
Fumio MatsudaDepartment of Bioinformatic Engineering, Graduate School of Information Science and Technology, Osaka University, 1-5 Yamadaoka, Suita, Osaka, 565-0871, Japan. fmatsuda@bio.eng.osaka-u.ac.jp.
Kazutaka ShimboResearch Institute for Bioscience Products & Fine Chemicals. Ajinomoto Co, Inc. 1-1 Suzuki-cho, Kawasaki-ku, Kawasaki-shi, Kanagawa, 210-8681, Japan.
Akiko OnukiResearch Institute for Bioscience Products & Fine Chemicals. Ajinomoto Co, Inc. 1-1 Suzuki-cho, Kawasaki-ku, Kawasaki-shi, Kanagawa, 210-8681, Japan.
Yousuke NishioResearch Institute for Bioscience Products & Fine Chemicals. Ajinomoto Co, Inc. 1-1 Suzuki-cho, Kawasaki-ku, Kawasaki-shi, Kanagawa, 210-8681, Japan.
Yoshihiro UsudaResearch Institute for Bioscience Products & Fine Chemicals. Ajinomoto Co, Inc. 1-1 Suzuki-cho, Kawasaki-ku, Kawasaki-shi, Kanagawa, 210-8681, Japan.
Akihiko KondoGraduate School of Science, Technology and Innovation, Kobe University, 1-1 Rokkodai, Nada, Kobe, 657-8501, Japan.
Jun IshiiGraduate School of Science, Technology and Innovation, Kobe University, 1-1 Rokkodai, Nada, Kobe, 657-8501, Japan. junjun@port.kobe-u.ac.jp.
Ajinomoto (Japan) · JPKobe University · JPSuzuki (Japan) · JPOsaka University · JP

Funding

New Energy and Industrial Technology Development Organization P16009
6 · The paper itself

Abstract

(-)-Carvone is a monoterpenoid with a spearmint flavor. A sustainable biotechnological production process for (-)-carvone is desirable. Although all enzymes in (-)-carvone biosynthesis have been functionally expressed in Escherichia coli independently, the yield was low in previous studies. When cytochrome P450 limonene-6-hydroxylase (P450)/cytochrome P450 reductase (CPR) and carveol dehydrogenase (CDH) were expressed in a single strain, by-product formation (dihydrocarveol and dihydrocarvone) was detected. We hypothesized that P450 and CDH expression levels differ in E. coli. Thus, two strains independently expressing P450/CPR and CDH were mixed with different ratios, confirming increased carvone production and decreased by-product formation when CDH input was reduced. The optimum ratio of enzyme expression to maximize (-)-carvone production was determined using the proteome analysis quantification concatamer (QconCAT) method. Thereafter, a single strain expressing both P450/CPR and CDH was constructed to imitate the optimum expression ratio. The upgraded strain showed a 15-fold improvement compared to the initial strain, showing a 44 ± 6.3 mg/L (-)-carvone production from 100 mg/L (-)-limonene. Our study showed the usefulness of the QconCAT proteome analysis method for strain development in the industrial biotechnology field.

Indexed as

Alcohol OxidoreductasesCyclohexane MonoterpenesCytochrome P-450 Enzyme SystemEscherichia coliLimoneneMonoterpenesNADPH-Ferrihemoprotein ReductasePlant ProteinsProteomeAlcohol Oxidoreductasescarveol dehydrogenasecarvoneCyclohexane MonoterpenesCytochrome P-450 Enzyme SystemdihydrocarvoneLimonenelimonene-6-hydroxylaseMonoterpenesNADPH-Ferrihemoprotein ReductasePlant ProteinsProteome

Identifiers

PMID34764337
PMCPMC8586248
OpenAlexW3212886274

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.