Evidence map›Paper›PMID 32369187›Full record

ArticleBiotechnology and bioengineering2020

Process intensification for cytochrome P450 BM3-catalyzed oxy-functionalization of dodecanoic acid.

Moritz B Buergler, Alexander Dennig, Bernd Nidetzky

Open access · hybridAbstract read
In one paragraph

Article in Biotechnology and bioengineering, 2020. 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
2.7field-weighted citation impact, top 11% 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, 21 citations in OpenAlex.

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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

3 authors at 1 institution in 1 country.

Moritz B BuerglerInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, Graz, Austria.
Alexander DennigInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, Graz, Austria.
Bernd NidetzkyInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, Graz, Austria.ORCID 0000-0002-5030-2643
Graz University of Technology · AT

Funding

Österreichische Forschungsförderungsgesellschaft
6 · The paper itself

Abstract

Selective oxy-functionalization of nonactivated C-H bonds is a long-standing "dream reaction" of organic synthesis for which chemical methodology is not well developed. Mono-oxygenase enzymes are promising catalysts for such oxy-functionalization to establish. Limitation on their applicability arises from low reaction output. Here, we showed an integrated approach of process engineering to the intensification of the cytochrome P450 BM3-catalyzed hydroxylation of dodecanoic acid (C12:0). Using P450 BM3 together with glucose dehydrogenase for regeneration of nicotinamide adenine dinucleotide phosphate (NADPH), we compared soluble and co-immobilized enzymes in O

Indexed as

Lauric AcidsBacterial ProteinsBiotechnologyCytochrome P-450 Enzyme SystemEnzymes, ImmobilizedNADPNADPH-Ferrihemoprotein ReductaseOxygenRecombinant Fusion ProteinsBacterial ProteinsCytochrome P-450 Enzyme SystemEnzymes, Immobilizedflavocytochrome P450 BM3 monoxygenaseslauric acidLauric AcidsNADPNADPH-Ferrihemoprotein ReductaseOxygenRecombinant Fusion Proteinscytochrome P450 BM3hydroxylationmono-oxygenaseprocess controlprocess engineeringprocess intensification

Identifiers

PMID32369187
PMCPMC7384007
OpenAlexW3021883061

What OpenQuestion holds

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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.