Evidence map›Paper›PMID 27878983›Full record

ArticleChemSusChem2017

Enzymatic Specific Production and Chemical Functionalization of Phenylpropanone Platform Monomers from Lignin.

Yukari Ohta, Ryoichi Hasegawa, Kanako Kurosawa, Allyn H Maeda, Toshio Koizumi, Hiroshi Nishimura, Hitomi Okada, Chen Qu, Kaori Saito, Takashi Watanabe and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in ChemSusChem, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

12 citing papers in PubMed, 56 citations in OpenAlex.

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  6. A heterodimeric glutathioneThe Journal of biological chemistry · 2019
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  10. Applied and environmental microbiology · 2018
    Article
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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

11 authors at 4 institutions in 1 country.

Yukari OhtaResearch and Development Center for Marine Biosciences, Japan Agency for Marine-Earth Science and Technology, JAMSTEC, 2-15 Natsushima, Yokosuka, Kanagawa, 237-0061, Japan.
Ryoichi HasegawaResearch and Development Center for Marine Biosciences, Japan Agency for Marine-Earth Science and Technology, JAMSTEC, 2-15 Natsushima, Yokosuka, Kanagawa, 237-0061, Japan.
Kanako KurosawaResearch and Development Center for Marine Biosciences, Japan Agency for Marine-Earth Science and Technology, JAMSTEC, 2-15 Natsushima, Yokosuka, Kanagawa, 237-0061, Japan.
Allyn H MaedaResearch and Development Center for Marine Biosciences, Japan Agency for Marine-Earth Science and Technology, JAMSTEC, 2-15 Natsushima, Yokosuka, Kanagawa, 237-0061, Japan.
Toshio KoizumiDepartment of Applied Chemistry, National Defense Academy, 1-10-20 Hashirimizu, Yokosuka, Kanagawa, 239-8686, Japan.
Hiroshi NishimuraResearch Institute for Sustainable Humanosphere, RISH, Kyoto University, Gokasho, Uji, Kyoto, 611-0011, Japan.
Hitomi OkadaResearch Institute for Sustainable Humanosphere, RISH, Kyoto University, Gokasho, Uji, Kyoto, 611-0011, Japan.
Chen QuResearch Institute for Sustainable Humanosphere, RISH, Kyoto University, Gokasho, Uji, Kyoto, 611-0011, Japan.
Kaori SaitoResearch Institute for Sustainable Humanosphere, RISH, Kyoto University, Gokasho, Uji, Kyoto, 611-0011, Japan.
Takashi WatanabeResearch Institute for Sustainable Humanosphere, RISH, Kyoto University, Gokasho, Uji, Kyoto, 611-0011, Japan.
Yuji HatadaDepartment of Life Sciences and Green Chemistry, Saitama Institute of Technology, 1690 Fusaiji, Fukaya, Saitama, 369-0293, Japan.
Kyoto University · JPJapan Agency for Marine-Earth Science and Technology · JPNational Defense Academy of Japan · JPSaitama Institute of Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzymatic catalysis is an ecofriendly strategy for the production of high-value low-molecular-weight aromatic compounds from lignin. Although well-definable aromatic monomers have been obtained from synthetic lignin-model dimers, enzymatic-selective synthesis of platform monomers from natural lignin has not been accomplished. In this study, we successfully achieved highly specific synthesis of aromatic monomers with a phenylpropane structure directly from natural lignin using a cascade reaction of β-O-4-cleaving bacterial enzymes in one pot. Guaiacylhydroxylpropanone (GHP) and the GHP/syringylhydroxylpropanone (SHP) mixture are exclusive monomers from lignin isolated from softwood (Cryptomeria japonica) and hardwood (Eucalyptus globulus). The intermediate products in the enzymatic reactions show the capacity to accommodate highly heterologous substrates at the substrate-binding sites of the enzymes. To demonstrate the applicability of GHP as a platform chemical for bio-based industries, we chemically generate value-added GHP derivatives for bio-based polymers. Together with these chemical conversions for the valorization of lignin-derived phenylpropanone monomers, the specific and enzymatic production of the monomers directly from natural lignin is expected to provide a new stream in "white biotechnology" for sustainable biorefineries.

Indexed as

BiocatalysisAcetoneCryptomeriaEucalyptusGlutathione TransferaseHydrogen-Ion ConcentrationLigninPropiophenonesTemperatureAcetoneGlutathione TransferaseLigninPropiophenonesbiomassenzymesligninmolecular recognitionreaction mechanisms

Identifiers

PMID27878983
PMCPMC5299523
OpenAlexW2551952924

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.