Evidence map›Paper›PMID 35807351›Full record

ArticleMolecules (Basel, Switzerland)2022

Improvement in the Thermostability of a Recombinant β-Glucosidase Immobilized in Zeolite under Different Conditions.

Luis Gerardo Ramírez-Ramírez, David Enrique Zazueta-Álvarez, Héctor Alonso Fileto-Pérez, Damián Reyes-Jáquez, Cynthia Manuela Núñez-Núñez, Juan de Dios Galindo-De la Rosa, Javier López-Miranda, Perla Guadalupe Vázquez-Ortega

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
1.0field-weighted citation impact, top 27% 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, 12 citations in OpenAlex.

  1. Article
  2. 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

8 authors at 3 institutions in 1 country.

Luis Gerardo Ramírez-RamírezDepartamento de Ingenierías Química y Bioquímica, Tecnológico Nacional de México (TecNM)-Instituto Tecnológico de Durango (ITD), Durango 34080, Mexico.ORCID 0000-0002-0541-2675
David Enrique Zazueta-ÁlvarezDepartamento de Ingeniería en Tecnología Ambiental, Universidad Politécnica de Durango, Durango 34300, Mexico.ORCID 0000-0002-6850-3988
Héctor Alonso Fileto-PérezDepartamento de Ingenierías Química y Bioquímica, Tecnológico Nacional de México (TecNM)-Instituto Tecnológico de Durango (ITD), Durango 34080, Mexico.
Damián Reyes-JáquezDepartamento de Ingenierías Química y Bioquímica, Tecnológico Nacional de México (TecNM)-Instituto Tecnológico de Durango (ITD), Durango 34080, Mexico.ORCID 0000-0002-6033-8965
Cynthia Manuela Núñez-NúñezDepartamento de Ingeniería en Tecnología Ambiental, Universidad Politécnica de Durango, Durango 34300, Mexico.
Juan de Dios Galindo-De la RosaDivisión de Investigación y Posgrado, Facultad de Ingeniería, Universidad Autónoma de Querétaro, Centro Universitario, Querétaro 76010, Mexico.
Javier López-MirandaDepartamento de Ingenierías Química y Bioquímica, Tecnológico Nacional de México (TecNM)-Instituto Tecnológico de Durango (ITD), Durango 34080, Mexico.
Perla Guadalupe Vázquez-OrtegaDepartamento de Ingenierías Química y Bioquímica, Tecnológico Nacional de México (TecNM)-Instituto Tecnológico de Durango (ITD), Durango 34080, Mexico.ORCID 0000-0003-2052-9799
Durango Institute of Technology · MXUniversidad Pedagógica de Durango · MXAutonomous University of Queretaro · MX

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

β-Glucosidase is part of the cellulases and is responsible for degrading cellobiose into glucose, a compound that can be used to produce biofuels. However, the use of the free enzyme makes the process more expensive. Enzyme immobilization improves catalytic characteristics and supports, such as zeolites, which have physical-chemical characteristics and ion exchange capacity that have a promising application in the biotechnological industry. This research aimed to immobilize by adsorption a recombinant β-glucosidase from

Indexed as

beta-GlucosidaseZeolitesEnzymes, ImmobilizedEnzyme StabilityHydrogen-Ion ConcentrationHydrolysisTemperaturebeta-GlucosidaseEnzymes, ImmobilizedZeolitesenzyme immobilizationenzyme stabilityzeoliteβ-glucosidases

Identifiers

PMID35807351
PMCPMC9268045
OpenAlexW4283582342

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.