Evidence map›Paper›PMID 40651038›Full record

ArticleChemistry & biodiversity2025

Recombinant Expression and Bioprocess Optimization of Priestia megaterium α-Amylase and Its Impact on Dough Fermentation Efficiency.

Atacan Erdem, Kübra Akbulut, Mustafa Türker, Barış Binay

Abstract read
In one paragraph

Article in Chemistry & biodiversity, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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.

Atacan ErdemPak Gıda Üretim ve Pazarlama A.Ş., Kocaeli, Türkiye.ORCID https://orcid.org/0000-0001-8590-3847
Kübra AkbulutDepartment of Bioengineering, Gebze Technical University, Gebze, Kocaeli, Türkiye.ORCID https://orcid.org/0000-0001-8705-405X
Mustafa TürkerPak Gıda Üretim ve Pazarlama A.Ş., Kocaeli, Türkiye.ORCID https://orcid.org/0000-0003-2327-4736
Barış BinayDepartment of Bioengineering, Gebze Technical University, Gebze, Kocaeli, Türkiye.ORCID https://orcid.org/0000-0002-6190-6549

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-Amylase is a key hydrolytic enzyme in starch degradation, playing a crucial role in industrial bioprocesses such as dough fermentation. However, optimizing α-amylase production remains challenging due to variations in microbial sources, culture conditions, and induction strategies. In this study, Priestia megaterium α-amylase (PmAmy) production was optimized for the first time based on the biomass/IPTG ratio in a controlled bioprocess. The impact of enzyme supplementation with equal quantity and enzymatic activity on dough fermentation was also evaluated to ensure consistent performance and effective application. Under the bioprocess conditions of 1.0 vvm airflow, 37°C, and 1000 rpm, a biomass-to-IPTG ratio was optimized as 20 g

Indexed as

alpha-AmylasesFermentationSaccharomycetalesBiomassRecombinant Proteinsalpha-AmylasesRecombinant Proteinsbiomassenzymesfermentation kinetics, Priestia megateriumα‐amylase

Identifiers

PMID40651038
PMCPMC12629164

What OpenQuestion holds

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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.