Evidence map›Paper›PMID 38791124›Full record

ArticleInternational journal of molecular sciences2024

A New Approach in Lipase-Octyl-Agarose Biocatalysis of 2-Arylpropionic Acid Derivatives.

Joanna Siódmiak, Jacek Dulęba, Natalia Kocot, Rafał Mastalerz, Gudmundur G Haraldsson, Michał Piotr Marszałł, Tomasz Siódmiak

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

7 authors.

Joanna SiódmiakDepartment of Laboratory Medicine, Faculty of Pharmacy, Ludwik Rydygier Collegium Medicum, Nicolaus Copernicus University in Toruń, 85-094 Bydgoszcz, Poland.
Jacek DulębaDepartment of Medicinal Chemistry, Faculty of Pharmacy, Collegium Medicum in Bydgoszcz, Nicolaus Copernicus University in Toruń, 85-089 Bydgoszcz, Poland.ORCID 0000-0003-1322-3820
Natalia KocotDepartment of Medicinal Chemistry, Faculty of Pharmacy, Collegium Medicum in Bydgoszcz, Nicolaus Copernicus University in Toruń, 85-089 Bydgoszcz, Poland.ORCID 0000-0001-9107-263X
Rafał MastalerzDepartment of Medicinal Chemistry, Faculty of Pharmacy, Collegium Medicum in Bydgoszcz, Nicolaus Copernicus University in Toruń, 85-089 Bydgoszcz, Poland.ORCID 0000-0002-8111-8945
Gudmundur G HaraldssonScience Institute, University of Iceland, 107 Reykjavik, Iceland.ORCID 0000-0002-5664-2745
Michał Piotr MarszałłDepartment of Medicinal Chemistry, Faculty of Pharmacy, Collegium Medicum in Bydgoszcz, Nicolaus Copernicus University in Toruń, 85-089 Bydgoszcz, Poland.
Tomasz SiódmiakDepartment of Medicinal Chemistry, Faculty of Pharmacy, Collegium Medicum in Bydgoszcz, Nicolaus Copernicus University in Toruń, 85-089 Bydgoszcz, Poland.ORCID 0000-0002-9232-5798

Funding

Nicolaus Copernicus University Excellence Initiative - Debuts, under the "Excellence Initiative-Research University" program, NCU in Toruń - 9/2022/Debiuty3 and 6/2022/Debiuty3
6 · The paper itself

Abstract

The use of lipase immobilized on an octyl-agarose support to obtain the optically pure enantiomers of chiral drugs in reactions carried out in organic solvents is a great challenge for chemical and pharmaceutical sciences. Therefore, it is extremely important to develop optimal procedures to achieve a high enantioselectivity of the biocatalysts in the organic medium. Our paper describes a new approach to biocatalysis performed in an organic solvent with the use of CALB-octyl-agarose support including the application of a polypropylene reactor, an appropriate buffer for immobilization (Tris base-pH 9, 100 mM), a drying step, and then the storage of immobilized lipases in a climatic chamber or a refrigerator. An immobilized lipase B from

Indexed as

BiocatalysisEnzymes, ImmobilizedFungal ProteinsLipaseSepharoseCandidaEnzyme StabilityEsterificationKineticsPropionatesSaccharomycetalesSolventsStereoisomerismTemperatureEnzymes, ImmobilizedFungal ProteinsLipaselipase B, Candida antarcticaPropionatesSepharoseSolventsclimatic chamberenantioselective esterificationimmobilizationkinetic resolutionlipase B from Candida antarcticalipase from Candida rugosaoctyl-agaroseoctyl-Sepharose CL-4Bpolypropylenereactor material(R,S)-flurbiprofenstorage stability

Identifiers

PMID38791124
PMCPMC11121684

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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.