Evidence map›Paper›PMID 36370158›Full record

ArticleApplied microbiology and biotechnology2022

Characterization and stabilization of the α-L-fucosidase set from Lacticaseibacillus rhamnosus INIA P603.

José Antonio Curiel, Ángela Peirotén, Susana Langa, Estela de Vega, Laura Blasco, José María Landete

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Applied microbiology and biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.9field-weighted citation impact, top 29% 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

2 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

José Antonio CurielDepartamento de Tecnología de Alimentos, Instituto Nacional de Investigación Y Tecnología Agraria Y Alimentaria (INIA-CSIC), Carretera de La Coruña Km 7.5, 28040, Madrid, Spain. joseantonio.curiel@inia.csic.es.ORCID http://orcid.org/0000-0002-0111-1437
Ángela PeiroténDepartamento de Tecnología de Alimentos, Instituto Nacional de Investigación Y Tecnología Agraria Y Alimentaria (INIA-CSIC), Carretera de La Coruña Km 7.5, 28040, Madrid, Spain.
Susana LangaDepartamento de Tecnología de Alimentos, Instituto Nacional de Investigación Y Tecnología Agraria Y Alimentaria (INIA-CSIC), Carretera de La Coruña Km 7.5, 28040, Madrid, Spain.
Estela de VegaUnidad de Servicio de Técnicas Analíticas, Instituto de Ciencia Y Tecnología de Alimentos Y Nutrición (ICTAN-CSIC), Calle José Antonio Nováis, 10, 28040, Madrid, Spain.
Laura BlascoDepartamento de Tecnología de Alimentos, Instituto Nacional de Investigación Y Tecnología Agraria Y Alimentaria (INIA-CSIC), Carretera de La Coruña Km 7.5, 28040, Madrid, Spain.
José María LandeteDepartamento de Tecnología de Alimentos, Instituto Nacional de Investigación Y Tecnología Agraria Y Alimentaria (INIA-CSIC), Carretera de La Coruña Km 7.5, 28040, Madrid, Spain.
Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria · ESInstituto de Ciencia y Tecnología de Alimentos y Nutrición · ES

Funding

Ministerio de Ciencia e Innovación PID2020-119630RB-I00Ministerio de Ciencia e Innovación RYC2019-026368-I
6 · The paper itself

Abstract

This study describes the molecular identification, biochemical characterization, and stabilization of three recombinant AlfA, AlfB, and AlfC fucosidases from Lacticaseibacillus rhamnosus INIA P603. Even though previous studies revealed the presence of fucosidase activity in L. rhamnosus extracts, the identification of the fucosidases, their physicochemical properties, and the substrate spectrum remained unknown. Although the presence of alfB is not common in strains of L. rhamnosus, fucosidases from L. rhamnosus INIA P603 were selected because this strain exhibited higher fucosidase activity in culture and the complete set of fucosidases. A high yield of purified recombinant AlfA, AlfB, and AlfC fucosidases was obtained (8, 12, and 18 mg, respectively). AlfA, AlfB, and AlfC showed their optimal activities at pH 5.0 and 4.0 at 60 °C, 40 °C, and 50 °C, respectively. Unlike 3-fucosyllactose, all three recombinant fucosidases were able to hydrolyze 2'-fucosyllactose (2'-FL), and their activities were improved through their immobilization on agarose supports. Nevertheless, immobilized AlfB exhibited the highest hydrolysis, releasing 39.6 µmol of fucose mg enzyme

Indexed as

alpha-L-FucosidaseLacticaseibacillus rhamnosusLacticaseibacillusalpha-L-Fucosidase2′-FucosyllactoseAlfBLacticaseibacillus rhamnosusLactose transfucosylationα-L-Fucosidase

Identifiers

PMID36370158
PMCPMC11621143
OpenAlexW4308834834

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.