Evidence map›Paper›PMID 39063171›Full record

ArticleInternational journal of molecular sciences2024

Recombinant Expression and Characterization of a Novel Thermo-Alkaline Lipase with Increased Solvent Stability from the Antarctic Thermophilic Bacterium

Diego Salas-Bruggink, Hardy Guzmán, Giannina Espina, Jenny M Blamey

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

4 authors.

Diego Salas-BrugginkFundación Biociencia, José Domingo Cañas 2280, Santiago 7750132, Chile.ORCID 0009-0004-1498-6509
Hardy GuzmánFacultad de Química y Biología, Universidad de Santiago de Chile, Alameda 3363, Santiago 9170022, Chile.
Giannina EspinaFundación Biociencia, José Domingo Cañas 2280, Santiago 7750132, Chile.ORCID 0000-0002-6308-7217
Jenny M BlameyFundación Biociencia, José Domingo Cañas 2280, Santiago 7750132, Chile.

Funding

Agencia Nacional de Investigación y Desarrollo ANID Proyecto de Exploración 2022 13220108
6 · The paper itself

Abstract

Lipases are enzymes that hydrolyze long-chain carboxylic esters, and in the presence of organic solvents, they catalyze organic synthesis reactions. However, the use of solvents in these processes often results in enzyme denaturation, leading to a reduction in enzymatic activity. Consequently, there is significant interest in identifying new lipases that are resistant to denaturing conditions, with extremozymes emerging as promising candidates for this purpose. Lip7, a lipase from

Indexed as

Enzyme StabilityGeobacillusLipaseRecombinant ProteinsSolventsAntarctic RegionsBacterial ProteinsEscherichia coliHydrogen-Ion ConcentrationKineticsSubstrate SpecificityTemperatureBacterial ProteinsLipaseRecombinant ProteinsSolventsbiocatalystbiotechnologyesteraseextremophileextremozymeprotein purification

Identifiers

PMID39063171
PMCPMC11277018

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.