Evidence map›Paper›PMID 35765016›Full record

ArticleJournal of biological engineering2022

Cloning, expression, and one-step purification/immobilization of two carbohydrate-binding module-tagged alcohol dehydrogenases.

Mario Benito, Ramón Román, Garazi Ortiz, Antoni Casablancas, Gregorio Álvaro, Gloria Caminal, Gloria González, Marina Guillén

Open access · goldAbstract read
In one paragraph

Article in Journal of biological engineering, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

5 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
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  4. Lactic Acid from COEnvironmental science & technology · 2023
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  5. Review
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

8 authors at 2 institutions in 1 country.

Mario BenitoBioprocess Engineering and Applied Biocatalysis Group, Department of Chemical Biological and Environmental Engineering, Universitat Autònoma de Barcelona, 08193, Bellaterra, Spain.
Ramón RománBioprocess Engineering and Applied Biocatalysis Group, Department of Chemical Biological and Environmental Engineering, Universitat Autònoma de Barcelona, 08193, Bellaterra, Spain.
Garazi OrtizBioprocess Engineering and Applied Biocatalysis Group, Department of Chemical Biological and Environmental Engineering, Universitat Autònoma de Barcelona, 08193, Bellaterra, Spain.
Antoni CasablancasBioprocess Engineering and Applied Biocatalysis Group, Department of Chemical Biological and Environmental Engineering, Universitat Autònoma de Barcelona, 08193, Bellaterra, Spain.
Gregorio ÁlvaroBioprocess Engineering and Applied Biocatalysis Group, Department of Chemical Biological and Environmental Engineering, Universitat Autònoma de Barcelona, 08193, Bellaterra, Spain.
Gloria CaminalInstitute of Advanced Chemistry of Catalonia, IQAC-CSIC, Jordi Girona 18-26, 08034, Barcelona, Spain.
Gloria GonzálezBioprocess Engineering and Applied Biocatalysis Group, Department of Chemical Biological and Environmental Engineering, Universitat Autònoma de Barcelona, 08193, Bellaterra, Spain. gloria.gonzalez@uab.cat.
Marina GuillénBioprocess Engineering and Applied Biocatalysis Group, Department of Chemical Biological and Environmental Engineering, Universitat Autònoma de Barcelona, 08193, Bellaterra, Spain.
Universitat Autònoma de Barcelona · ESInstitute of Advanced Chemistry of Catalonia · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe feasibility of biochemical transformation processes is usually greatly dependent on biocatalysts cost. Therefore, immobilizing and reusing biocatalysts is an approach to be considered to bring biotransformations closer to industrial feasibility, since it does not only allow to reuse enzymes but can also improve their stability towards several reaction conditions. Carbohydrate-Binding Modules (CBM) are well-described domains involved in substrate binding which have been already used as purification tags.

resultsIn this work, two different Carbohydrate-Binding Modules (CBM3 and CBM9) have been successfully fused to an alcohol dehydrogenase from Saccharomyces cerevisiae, which has been produced in bench-scale reactor using an auxotrophic M15-derived E. coli strain, following a fed-batch strategy with antibiotic-free medium. Around 40 mg·g

conclusionCBM domains were proved to be suitable for one-step immobilization/purification process, retaining almost total activity offered. However, purification process was only successful with CBM9.

Indexed as

Alcohol dehydrogenaseCarbohydrate-binding moduleEscherichia coliOne-step immobilization/purificationRegenerated amorphous cellulose

Identifiers

PMID35765016
PMCPMC9241262
OpenAlexW4283695377

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.