Evidence map›Paper›PMID 33026494›Full record

ArticleApplied microbiology and biotechnology2020

Chitosan-based CLEAs from Aspergillus niger type A feruloyl esterase: high-productivity biocatalyst for alkyl ferulate synthesis.

Daniel Grajales-Hernández, Mariana Armendáriz-Ruiz, Susana Velasco-Lozano, Fernando López-Gallego, Juan Carlos Mateos-Díaz

Abstract read
PubMed Publisher
In one paragraph

Article in Applied microbiology and biotechnology, 2020. 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
1.1field-weighted citation impact, top 23% 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, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. An alginate-confined peroxygenase-CLEA for styrene epoxidation.Chemical communications (Cambridge, England) · 2021
    Article
  4. Review
  5. 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

5 authors at 2 institutions in 2 countries.

Daniel Grajales-HernándezIndustrial Biotechnology Unit, Centro de Investigación y Asistencia en Tecnología y Diseño del Estado de Jalisco A.C., Av. Normalistas, 800, Guadalajara, Mexico.
Mariana Armendáriz-RuizIndustrial Biotechnology Unit, Centro de Investigación y Asistencia en Tecnología y Diseño del Estado de Jalisco A.C., Av. Normalistas, 800, Guadalajara, Mexico.
Susana Velasco-LozanoHeterogeneous Biocatalysis Laboratory. Center for Cooperative Research in Biomaterials (CIC biomaGUNE), Basque Research and Technology Alliance (BRTA), Paseo de Miramon 182, 20014, Donostia San Sebastián, Spain.
Fernando López-GallegoHeterogeneous Biocatalysis Laboratory. Center for Cooperative Research in Biomaterials (CIC biomaGUNE), Basque Research and Technology Alliance (BRTA), Paseo de Miramon 182, 20014, Donostia San Sebastián, Spain.
Juan Carlos Mateos-DíazIndustrial Biotechnology Unit, Centro de Investigación y Asistencia en Tecnología y Diseño del Estado de Jalisco A.C., Av. Normalistas, 800, Guadalajara, Mexico. jcmateos@ciatej.mx.ORCID http://orcid.org/0000-0002-6723-6654
Secretaría de Salud de Jalisco · MXCIC biomaGUNE · ES

Funding

Consejo Nacional de Ciencia y Tecnología (MX) 2017-01-6267Ikerbasque, Basque Foundation for Science BIO2015-69887-RMinisterio de Economía, Industria y Competitividad, Gobierno de España RTI2018-094398-B-I00
6 · The paper itself

Abstract

The enzymatic synthesis of alkyl ferulates is an important reaction in cosmetic and pharmaceutical chemistries, since it may allow to expand the biorefinery concept valorizing biomass wastes enriched in ferulic acid. However, robust biocatalysts for that purpose are scarce. Herein, we have immobilized the type A feruloyl esterase from Aspergillus niger (AnFaeA) as cross-linked enzyme aggregates, employing chitosan as co-feeder (ChCLEAs). High immobilization yields and relative activity recovery were attained in all assessed conditions (> 93%). Furthermore, we enhanced the thermal stability of the soluble enzyme 32-fold. AnFaeA-ChCLEAs were capable to quantitatively perform the solvent-free direct esterification of short- to medium-chain alkyl ferulates (C4-C12) in less than 24 h. By raising the operational temperature to 50 °C, AnFaeA-ChCLEAs transformed 350 mM ferulic acid into isopentyl ferulate with a space-time yield of 46.1 g of product × L

Indexed as

Aspergillus nigerChitosanCarboxylic Ester HydrolasesCarboxylic Ester HydrolasesChitosanferuloyl esteraseAlkyl ferulatesEnzyme immobilizationEnzymesEsterasesHeterogeneous biocatalysts

Identifiers

PMID33026494
OpenAlexW3092074368

What OpenQuestion holds

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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.