Evidence map›Paper›PMID 42074144›Full record

ArticleInternational journal of molecular sciences2026

Ultrasound-Assisted Optimization of the Activation and Inactivation of Thermostable α-Amylase.

Zahra Azzouz, Ourdia-Nouara Kernou, Naima Djerroud-Mohellebi, Festus Ogungbemiro, Zahir Amghar, Nassima Kichi, Azzeddine Bettache, Nawel Boucherba, Samir Hadjal, Patricia Rijo

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2026. 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
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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

10 authors.

Zahra AzzouzLaboratoire de Microbiologie Appliquée (LMA), Faculté des Sciences de la Nature et de la Vie, Université de Bejaia, Bejaia 06000, Algeria.ORCID 0000-0001-5524-238X
Ourdia-Nouara KernouLaboratoire de Biomathématiques, Biophysique, Biochimie et Scientométrie (L3BS), Faculté des Sciences de la Nature et de la Vie, Université de Bejaia, Bejaia 06000, Algeria.
Naima Djerroud-MohellebiDépartement Ecologie et Environnement, Faculté des Sciences Biologiques, Université des Sciences et de la Technologie Houari Boumediene USTHB Bab-Ezzouar, Alger 16111, Algeria.
Festus OgungbemiroCBIOS-Centro de Investigação em Biociências e Tecnologias da Saúde, Universidade Lusófona, 1749-024 Lisboa, Portugal.
Zahir AmgharLaboratoire de Microbiologie Appliquée (LMA), Faculté des Sciences de la Nature et de la Vie, Université de Bejaia, Bejaia 06000, Algeria.ORCID 0009-0004-3318-4456
Nassima KichiLaboratoire de Microbiologie Appliquée (LMA), Faculté des Sciences de la Nature et de la Vie, Université de Bejaia, Bejaia 06000, Algeria.
Azzeddine BettacheLaboratoire de Microbiologie Appliquée (LMA), Faculté des Sciences de la Nature et de la Vie, Université de Bejaia, Bejaia 06000, Algeria.
Nawel BoucherbaLaboratoire de Microbiologie Appliquée (LMA), Faculté des Sciences de la Nature et de la Vie, Université de Bejaia, Bejaia 06000, Algeria.ORCID 0000-0002-7273-1019
Samir HadjalLaboratoire de Recherche et Développement Produit, Direction de Recherche et Développement, Cevital Agro-Industrie, Nouveau Quai Port de Bejaia, Bejaia 06000, Algeria.
Patricia RijoCBIOS-Centro de Investigação em Biociências e Tecnologias da Saúde, Universidade Lusófona, 1749-024 Lisboa, Portugal.ORCID 0000-0001-7992-8343

Funding

Fundação para a Ciência e a Tecnologia (FCT, Portugal) https://doi.org/10.54499/UID/04567/2025
6 · The paper itself

Abstract

Ultrasound is a non-thermal technology increasingly applied in food processing to modulate enzyme activity. This study investigated the effects of ultrasonic irradiation on the activity of a commercial thermostable α-amylase. Enzyme activity was determined by quantifying reducing sugars released from starch using the 3,5-dinitrosalicylic acid method, and protein concentration was measured by the Bradford assay. A one-factor-at-a-time approach was used to evaluate the effects of ultrasonic amplitude, treatment time, enzyme concentration, incubation temperature, and calcium ion concentration. Subsequently, a Box-Behnken design was applied to analyze the combined influence of amplitude, treatment duration, temperature, and calcium concentration on residual activity. The enzyme exhibited an initial activity of 46.27 ± 3.63 U/mL under standard assay conditions. Moderate ultrasonic amplitudes enhanced activity, whereas prolonged exposure and elevated temperatures promoted inactivation. Statistical analysis showed that the incubation temperature and calcium concentration significantly influenced residual activity, and the quadratic model provided a good fit (R

Indexed as

alpha-AmylasesUltrasonic WavesCalciumEnzyme ActivationEnzyme StabilityHot TemperatureKineticsTemperaturealpha-AmylasesCalciumactivationinactivationoptimizationthermostable α-amylaseultrasound

Identifiers

PMID42074144
PMCPMC13116321

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Registered trials

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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.