Evidence map›Paper›PMID 42496064›Full record

ArticleChembiochem : a European journal of chemical biology2026

Continuous and Divergent Biotransformation of β-Ketoesters Into Enantiomerically Pure β-Hydroxyacids or Their Oligomers Through a Telescoped Multienzyme Cascade.

Giulio Pota, Daniel Andrés-Sanz, Ainhoa Maiz-Iginitz, Mariana A Armendáriz-Ruiz, Haritz Sardon, Giuseppe Vitiello, Valeria Califano, Aniello Costantini, Fernando López-Gallego

Abstract read
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In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2026. 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

9 authors.

Giulio PotaHeterogeneous Biocatalysis Laboratory, Center for Cooperative Research in Biomaterials (CIC biomaGUNE), Basque Research and Technology Alliance (BRTA), Donostia/San Sebastián, Spain.
Daniel Andrés-SanzHeterogeneous Biocatalysis Laboratory, Center for Cooperative Research in Biomaterials (CIC biomaGUNE), Basque Research and Technology Alliance (BRTA), Donostia/San Sebastián, Spain.
Ainhoa Maiz-IginitzHeterogeneous Biocatalysis Laboratory, Center for Cooperative Research in Biomaterials (CIC biomaGUNE), Basque Research and Technology Alliance (BRTA), Donostia/San Sebastián, Spain.
Mariana A Armendáriz-RuizHeterogeneous Biocatalysis Laboratory, Center for Cooperative Research in Biomaterials (CIC biomaGUNE), Basque Research and Technology Alliance (BRTA), Donostia/San Sebastián, Spain.
Haritz SardonPOLYMAT, Department of Polymer Science and Technology, University of the Basque Country UPV/EHU, Donostia/San Sebastian, Spain.
Giuseppe VitielloDepartment of Chemical, Materials and Production Engineering, University of Naples Federico II, Naples, Italy.
Valeria CalifanoInstitute of Science and Technology for Sustainable Energy and Mobility (STEMS), National Research Council of Italy (CNR), Naples, Italy.
Aniello CostantiniDepartment of Chemical, Materials and Production Engineering, University of Naples Federico II, Naples, Italy.
Fernando López-GallegoHeterogeneous Biocatalysis Laboratory, Center for Cooperative Research in Biomaterials (CIC biomaGUNE), Basque Research and Technology Alliance (BRTA), Donostia/San Sebastián, Spain.

Funding

Basque Government's Predoctoral Programme PRE_2024_2_0257ERC-Co METACELL-818089Horizon Research and Innovation Program under the Marie Sklodowska-Curie Actions 101204989Predoctoral Stays Program EP_2023_1_0086
6 · The paper itself

Abstract

Efficient, selective, and sustainable synthetic platforms are increasingly important in modern chemical manufacturing, yet chemical flexibility often remains limited. In this study, we develop a modular biocatalytic system for the divergent and continuous transformation of ethyl acetoacetate (EAA) into either enantiomerically pure (R)-3-hydroxybutyric acid ((R)-3HBA) or oligomers of (R)-poly(3-hydroxybutyrate) (PHB). The cascade combines two telescoped packed-bed reactors containing an immobilized, self-sufficient Lactobacillus kefir ketoreductase (LkKRED) and commercial immobilized Candida antarctica lipase B (N435). By simply tuning the reaction conditions, the system selectively directs the substrate toward either product. Under aqueous conditions, it achieves quantitative conversion to (R)-3HBA with >99% enantiomeric excess and maintains excellent stability over 7 days of continuous operation. It also reaches a maximum space-time yield of 105 g L

Indexed as

3-Hydroxybutyric AcidHydroxy AcidsHydroxybutyratesLipasePolyestersAcetoacetatesBiocatalysisBiotransformationContinuous Flow ChemistryEnzymes, ImmobilizedFungal ProteinsLactobacillusPolyhydroxybutyratesStereoisomerism3-Hydroxybutyric AcidAcetoacetatesEnzymes, Immobilizedethyl acetoacetateFungal ProteinsHydroxy AcidsHydroxybutyratesLipaselipase B, Candida antarcticapoly-beta-hydroxybutyratePolyestersPolyhydroxybutyratesdehydrogenasesflow biocatalysislipasespolycondensationself‐sufficient biocatalysts

Identifiers

PMID42496064
PMCPMC13398027

What OpenQuestion holds

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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.