Evidence map›Paper›PMID 41075049›Full record

ArticleBiotechnology letters2025

Production and application of α-amylase, native AmyJ33-ABC, from Bacillus siamensis JJC33M in gelatinized potato starch and its industrial potential.

Sarahi Hernández-Heredia, María Guadalupe Aguilar-Uscanga, Cirilo Nolasco-Hipólito, Sandra Del Moral

Abstract read
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In one paragraph

Article in Biotechnology letters, 2025. 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.

Sarahi Hernández-HerediaFood Research and Development Unit, National Institute of Technology of Mexico, Veracruz Institute of Technology, Miguel Ángel de Quevedo 2779, CP 91897, Veracruz, Mexico.
María Guadalupe Aguilar-UscangaFood Research and Development Unit, National Institute of Technology of Mexico, Veracruz Institute of Technology, Miguel Ángel de Quevedo 2779, CP 91897, Veracruz, Mexico.
Cirilo Nolasco-HipólitoInstitute of Biotechnology, University of Papaloapan, Circuito Central 200, CP 68301, Tuxtepec, Oaxaca, Mexico.
Sandra Del MoralFood Research and Development Unit, National Institute of Technology of Mexico, Veracruz Institute of Technology, Miguel Ángel de Quevedo 2779, CP 91897, Veracruz, Mexico. sandra.dv@veracruz.tecnm.mx.ORCID http://orcid.org/0000-0002-0496-2325

Funding

CONAHCYT 002026CONAHCYT PN-2017-4650
6 · The paper itself

Abstract

α-Amylases (EC 3.2.1.1) are endoenzymes that hydrolyze α-1,4-glycosidic bonds in starch to produce maltooligosaccharides with broad industrial applications (food, textile, fermentation, biofuels). Most α-amylases act only on gelatinized starch, but Bacillus siamensis JJC33M secretes a native enzyme (AmyJ33-ABC) active on both gelatinized and raw starch. The growth of B. siamensis JJC33M was evaluated, showing µ = 0.55 h⁻

Indexed as

alpha-AmylasesBacillusBacterial ProteinsSolanum tuberosumStarchEnzyme StabilityGelatinHydrogen-Ion ConcentrationKineticsOligosaccharidesTemperaturealpha-AmylasesBacterial ProteinsGelatinOligosaccharidesStarchB. siamensis JJ33MRaw starch hydrolysisSubstrate-binding sites (SBS)α-amylase

Identifiers

PMID41075049

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.