Evidence map›Paper›PMID 23542620›Full record

ArticleApplied and environmental microbiology2013

Biochemical diversity of carboxyl esterases and lipases from Lake Arreo (Spain): a metagenomic approach.

Mónica Martínez-Martínez, María Alcaide, Anatoli Tchigvintsev, Oleg Reva, Julio Polaina, Rafael Bargiela, María-Eugenia Guazzaroni, Alvaro Chicote, Albert Canet, Francisco Valero and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

19 citing papers in PubMed, 55 citations in OpenAlex.

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  10. Aii810, a Novel Cold-AdaptedFrontiers in microbiology · 2017
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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

14 authors at 7 institutions in 3 countries.

Mónica Martínez-MartínezSpanish National Research Council (CSIC), Department of Applied Biocatalysis, Institute of Catalysis, Madrid, Spain.
María Alcaide
Anatoli Tchigvintsev
Oleg Reva
Julio Polaina
Rafael Bargiela
María-Eugenia Guazzaroni
Alvaro Chicote
Albert Canet
Francisco Valero
Eugenio Rico Eguizabal
María del Carmen Guerrero
Alexander F Yakunin
Manuel Ferrer
Consejo Superior de Investigaciones Científicas · ESUniversidad Autónoma de Madrid · ESUniversitat Autònoma de Barcelona · ESUniversity of Toronto · CAInstituto de Agroquímica y Tecnología de Alimentos · ESUniversity of Castilla-La Mancha · ESUniversity of Pretoria · ZA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The esterases and lipases from the α/β hydrolase superfamily exhibit an enormous sequence diversity, fold plasticity, and activities. Here, we present the comprehensive sequence and biochemical analyses of seven distinct esterases and lipases from the metagenome of Lake Arreo, an evaporite karstic lake in Spain (42°46'N, 2°59'W; altitude, 655 m). Together with oligonucleotide usage patterns and BLASTP analysis, our study of esterases/lipases mined from Lake Arreo suggests that its sediment contains moderately halophilic and cold-adapted proteobacteria containing DNA fragments of distantly related plasmids or chromosomal genomic islands of plasmid and phage origins. This metagenome encodes esterases/lipases with broad substrate profiles (tested over a set of 101 structurally diverse esters) and habitat-specific characteristics, as they exhibit maximal activity at alkaline pH (8.0 to 8.5) and temperature of 16 to 40°C, and they are stimulated (1.5 to 2.2 times) by chloride ions (0.1 to 1.2 M), reflecting an adaptation to environmental conditions. Our work provides further insights into the potential significance of the Lake Arreo esterases/lipases for biotechnology processes (i.e., production of enantiomers and sugar esters), because these enzymes are salt tolerant and are active at low temperatures and against a broad range of substrates. As an example, the ability of a single protein to hydrolyze triacylglycerols, (non)halogenated alkyl and aryl esters, cinnamoyl and carbohydrate esters, lactones, and chiral epoxides to a similar extent was demonstrated.

Indexed as

Models, MolecularBiotechnologyCarboxylic Ester HydrolasesCloning, MolecularComputational BiologyHydrogen-Ion ConcentrationLakesLipaseMetagenomeMetagenomicsOligonucleotidesProteobacteriaSpainTemperatureCarboxylic Ester HydrolasesLipaseOligonucleotides

Identifiers

PMID23542620
PMCPMC3675924
OpenAlexW2135075544

What OpenQuestion holds

Textmetadata
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.