Evidence map›Paper›PMID 28464820›Full record

ArticleMicrobial cell factories2017

Purification and characterization of a novel cold adapted fungal glucoamylase.

Mario Carrasco, Jennifer Alcaíno, Víctor Cifuentes, Marcelo Baeza

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.3field-weighted citation impact, top 9% 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

17 citing papers in PubMed, 62 citations in OpenAlex.

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  12. Characterization of SdGA, a cold-adapted glucoamylase fromBiotechnology reports (Amsterdam, Netherlands) · 2021
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  14. Genome-Wide Transcriptional Changes ofFrontiers in microbiology · 2021
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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

4 authors at 1 institution in 1 country.

Mario CarrascoDepartamento de Ciencias Ecológicas, Facultad de Ciencias, Universidad de Chile, Las Palmeras 342, Casilla 653, Santiago, Chile.
Jennifer AlcaínoDepartamento de Ciencias Ecológicas, Facultad de Ciencias, Universidad de Chile, Las Palmeras 342, Casilla 653, Santiago, Chile.
Víctor CifuentesDepartamento de Ciencias Ecológicas, Facultad de Ciencias, Universidad de Chile, Las Palmeras 342, Casilla 653, Santiago, Chile.
Marcelo BaezaDepartamento de Ciencias Ecológicas, Facultad de Ciencias, Universidad de Chile, Las Palmeras 342, Casilla 653, Santiago, Chile. mbaeza@u.uchile.cl.
University of Chile · CL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundAmylases are used in various industrial processes and a key requirement for the efficiency of these processes is the use of enzymes with high catalytic activity at ambient temperature. Unfortunately, most amylases isolated from bacteria and filamentous fungi have optimal activity above 45 °C and low pH. For example, the most commonly used industrial glucoamylases, a type of amylase that degrades starch to glucose, are produced by Aspergillus strains displaying optimal activities at 45-60 °C. Thus, isolating new amylases with optimal activity at ambient temperature is essential for improving industrial processes. In this report, a glucoamylase secreted by the cold-adapted yeast Tetracladium sp. was isolated and biochemically characterized.

resultsThe effects of physicochemical parameters on enzyme activity were analyzed, and pH and temperature were found to be key factors modulating the glucoamylase activity. The optimal conditions for enzyme activity were 30 °C and pH 6.0, and the K

conclusionThe glucoamylase secreted by Tetracladium sp. is a novel cold-adapted enzyme and its properties should render this enzyme suitable for use in industrial processes that require cold-active amylases, such as biofuel production.

Indexed as

Cold TemperatureAdaptation, PhysiologicalAntarctic RegionsAscomycotaGlucan 1,4-alpha-GlucosidaseGlycosylationHydrogen-Ion ConcentrationKineticsModels, MolecularStarchSubstrate SpecificityGlucan 1,4-alpha-GlucosidaseStarchAntarctic fungiCold-adapted amylaseFungal amylaseTetracladium sp.

Identifiers

PMID28464820
PMCPMC5414198
OpenAlexW2610285500

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.