Evidence map›Paper›PMID 34111325›Full record

ArticleChemSusChem2021

Dual Valorization of Lignin as a Versatile and Renewable Matrix for Enzyme Immobilization and (Flow) Bioprocess Engineering.

Ana I Benítez-Mateos, Stefania Bertella, Jean Behaghel de Bueren, Jeremy S Luterbacher, Francesca Paradisi

Abstract read
In one paragraph

Article in ChemSusChem, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

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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

5 authors.

Ana I Benítez-MateosDepartment of Chemistry, Biochemistry and Pharmaceutical Sciences, University of Bern, Freiestrasse 3, 3012, Bern, Switzerland.
Stefania BertellaLaboratory of Sustainable and Catalytic Processing, Institute of Chemical Sciences and Engineering, École Polytechnique Fédérale de Lausanne (EPFL), 1015, Lausanne, Switzerland.
Jean Behaghel de BuerenLaboratory of Sustainable and Catalytic Processing, Institute of Chemical Sciences and Engineering, École Polytechnique Fédérale de Lausanne (EPFL), 1015, Lausanne, Switzerland.
Jeremy S LuterbacherLaboratory of Sustainable and Catalytic Processing, Institute of Chemical Sciences and Engineering, École Polytechnique Fédérale de Lausanne (EPFL), 1015, Lausanne, Switzerland.
Francesca ParadisiDepartment of Chemistry, Biochemistry and Pharmaceutical Sciences, University of Bern, Freiestrasse 3, 3012, Bern, Switzerland.ORCID http://orcid.org/0000-0003-1704-0642

Funding

University of Bern "Seal of Excellence Fund" Postdoctoral Fellowship 200021_192274University of Bern "Seal of Excellence Fund" Postdoctoral Fellowship CRSII5_180258University of Bern "Seal of Excellence Fund" Postdoctoral Fellowship SELF19-03 BIORPHANDRUG
6 · The paper itself

Abstract

Lignin has emerged as an attractive alternative in the search for more eco-friendly and less costly materials for enzyme immobilization. In this work, the terephthalic aldehyde-stabilization of lignin is carried out during its extraction to develop a series of functionalized lignins with a range of reactive groups (epoxy, amine, aldehyde, metal chelates). This expands the immobilization to a pool of enzymes (carboxylase, dehydrogenase, transaminase) by different binding chemistries, affording immobilization yields of 64-100 %. As a proof of concept, a ω-transaminase reversibly immobilized on polyethyleneimine-lignin is integrated in a packed-bed reactor. The stability of the immobilized biocatalyst is tested in continuous-flow deamination reactions and maintains the same conversion for 100 cycles. These results outperform previous stability tests carried out with the enzyme covalently immobilized on methacrylic resins, with the advantage that the reversibility of the immobilized enzyme allows recycling and reuse of lignin beyond the enzyme inactivation. Additionally, an in-line system also based on lignin is added into the downstream process to separate the reaction products by catch-and-release. These results demonstrate a fully closed-loop sustainable flow-biocatalytic system based exclusively on lignin.

Indexed as

biocatalysisenzyme immobilizationflow chemistryligninrenewable resources

Identifiers

PMID34111325
PMCPMC8457236

What OpenQuestion holds

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Registered trials

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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.