Evidence map›Paper›PMID 31727078›Full record

ReviewMicrobial cell factories2019

Laccases: structure, function, and potential application in water bioremediation.

Leticia Arregui, Marcela Ayala, Ximena Gómez-Gil, Guadalupe Gutiérrez-Soto, Carlos Eduardo Hernández-Luna, Mayra Herrera de Los Santos, Laura Levin, Arturo Rojo-Domínguez, Daniel Romero-Martínez, Mario C N Saparrat and 2 more

Abstract readReview
In one paragraph

Review in Microbial cell factories, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers.

0numbers the graph read from it
0cells of the map it votes in
123citing 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

123 citing papers in PubMed.

  1. Review
  2. Exploring the role of oxidative defects in polyethylene binding and degradation by a Rhodococcus opacus R7 multicopper oxidase: a computational perspective.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
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  7. Review
  8. Aggregation of Phosphates Enhances Enzyme Activity in Aqueous Solution.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026
    Article
  9. Chemo-Enzymatic Route for Covalent Cellulose Fiber Dyeing.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026
    Article
  10. Enhanced Inhibition ofInternational journal of molecular sciences · 2026
    Article
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63 more citing papers are in PubMed but not listed here.

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

12 authors.

Leticia ArreguiDepartamento de Ciencias Naturales, Universidad Autónoma Metropolitana, Unidad Cuajimalpa, Av. Vasco de Quiroga 4871, Col. Santa Fe Cuajimalpa, C.P. 05348, Mexico City, Mexico.
Marcela AyalaDepartamento de Ingeniería Celular y Biocatálisis, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Av. Universidad 2001 Chamilpa, 62210, Cuernavaca, Morelos, Mexico.
Ximena Gómez-GilPrograma de Investigación de Producción de Biomoléculas, Departamento de Biología Molecular y Biotecnología, Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México, AP. 70228, Mexico City, CP. 04510, Mexico.
Guadalupe Gutiérrez-SotoFacultad de Agronomía, Universidad Autónoma de Nuevo León, Francisco Villa, 66059 Colonia Ex hacienda El Canadá, General Escobedo, Nuevo León, Mexico.
Carlos Eduardo Hernández-LunaLaboratorio de Enzimología, Facultad de Ciencias Biológicas, Universidad Autónoma de Nuevo León, Pedro de Alba y Manuel L. Barragán, Cd. Universitaria, 66451, San Nicolás de los Garza, Nuevo León, Mexico.
Mayra Herrera de Los SantosPrograma de Investigación de Producción de Biomoléculas, Departamento de Biología Molecular y Biotecnología, Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México, AP. 70228, Mexico City, CP. 04510, Mexico.
Laura LevinLaboratorio de Micología Experimental, DBBE, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, INMIBO-CONICET, Ciudad Universitaria, Pabellón 2, Piso 4, C1428BGA, Ciudad Autónoma de Buenos Aires, Argentina.
Arturo Rojo-DomínguezDepartamento de Ciencias Naturales, Universidad Autónoma Metropolitana, Unidad Cuajimalpa, Av. Vasco de Quiroga 4871, Col. Santa Fe Cuajimalpa, C.P. 05348, Mexico City, Mexico.
Daniel Romero-MartínezPrograma de Investigación de Producción de Biomoléculas, Departamento de Biología Molecular y Biotecnología, Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México, AP. 70228, Mexico City, CP. 04510, Mexico.
Mario C N SaparratInstituto de Fisiología Vegetal (INFIVE), Universidad Nacional de La Plata (UNLP)-CCT-La Plata-Consejo Nacional de Investigaciones Científicas y técnicas (CONICET), Diag. 113 y 61, 327CC, 1900, La Plata, Argentina.
Mauricio A Trujillo-RoldánPrograma de Investigación de Producción de Biomoléculas, Departamento de Biología Molecular y Biotecnología, Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México, AP. 70228, Mexico City, CP. 04510, Mexico.
Norma A Valdez-CruzPrograma de Investigación de Producción de Biomoléculas, Departamento de Biología Molecular y Biotecnología, Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México, AP. 70228, Mexico City, CP. 04510, Mexico. adri@biomedicas.unam.mx.ORCID http://orcid.org/0000-0002-8581-1173

Funding

Programa Iberoamericano de Ciencia y Tecnología para el Desarrollo 318RT0552 - red LACASAS INMOVILIZADAS PARA LA DEGRADACIÓN DE COMPUESTOS AROMÁTICOS EN AGUAS RESIDUALES (LIDA)
6 · The paper itself

Abstract

The global rise in urbanization and industrial activity has led to the production and incorporation of foreign contaminant molecules into ecosystems, distorting them and impacting human and animal health. Physical, chemical, and biological strategies have been adopted to eliminate these contaminants from water bodies under anthropogenic stress. Biotechnological processes involving microorganisms and enzymes have been used for this purpose; specifically, laccases, which are broad spectrum biocatalysts, have been used to degrade several compounds, such as those that can be found in the effluents from industries and hospitals. Laccases have shown high potential in the biotransformation of diverse pollutants using crude enzyme extracts or free enzymes. However, their application in bioremediation and water treatment at a large scale is limited by the complex composition and high salt concentration and pH values of contaminated media that affect protein stability, recovery and recycling. These issues are also associated with operational problems and the necessity of large-scale production of laccase. Hence, more knowledge on the molecular characteristics of water bodies is required to identify and develop new laccases that can be used under complex conditions and to develop novel strategies and processes to achieve their efficient application in treating contaminated water. Recently, stability, efficiency, separation and reuse issues have been overcome by the immobilization of enzymes and development of novel biocatalytic materials. This review provides recent information on laccases from different sources, their structures and biochemical properties, mechanisms of action, and application in the bioremediation and biotransformation of contaminant molecules in water. Moreover, we discuss a series of improvements that have been attempted for better organic solvent tolerance, thermo-tolerance, and operational stability of laccases, as per process requirements.

Indexed as

BiocatalysisLaccaseBiodegradation, EnvironmentalEcosystemEnvironmental PollutantsFungiPlantsWaterWater PurificationEnvironmental PollutantsLaccaseWaterBioremediationEmerging contaminantsLaccasesWater bodies

Identifiers

PMID31727078
PMCPMC6854816

What OpenQuestion holds

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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.