Evidence map›Paper›PMID 40982022›Full record

ArticleBiotechnology letters2025

Molecular cloning and modelling of a thermostable α-amylase from a thermophilic Geobacillus sp. DS3.

Lucia Dhiantika Witasari, Leon Bhagawanta Cahyono, Dina Clarissa Kurniawan, Rohmad Yudi Utomo, Muhammad Nur Cahyanto, Muhammad Saifur Rohman, Irfan Dwidya Prijambada

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Article in Biotechnology letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. Review
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

7 authors.

Lucia Dhiantika WitasariDepartment of Food and Agriculture Products Technology, Faculty of Agricultural Technology, Universitas Gadjah Mada, Sleman, D.I. Yogyakarta, Indonesia. dhiantea_k@ugm.ac.id.ORCID http://orcid.org/0000-0001-9614-4540
Leon Bhagawanta CahyonoDepartment of Food and Agriculture Products Technology, Faculty of Agricultural Technology, Universitas Gadjah Mada, Sleman, D.I. Yogyakarta, Indonesia.
Dina Clarissa KurniawanDepartment of Food and Agriculture Products Technology, Faculty of Agricultural Technology, Universitas Gadjah Mada, Sleman, D.I. Yogyakarta, Indonesia.
Rohmad Yudi UtomoDepartment of Pharmaceutical Chemistry, Faculty of Pharmacy, UGM, Sleman, D.I. Yogyakarta, Indonesia.
Muhammad Nur CahyantoDepartment of Food and Agriculture Products Technology, Faculty of Agricultural Technology, Universitas Gadjah Mada, Sleman, D.I. Yogyakarta, Indonesia.
Muhammad Saifur RohmanDepartment of Agricultural Microbiology, Faculty of Agriculture, Universitas Gadjah Mada, Sleman, D.I. Yogyakarta, Indonesia.
Irfan Dwidya PrijambadaDepartment of Agricultural Microbiology, Faculty of Agriculture, Universitas Gadjah Mada, Sleman, D.I. Yogyakarta, Indonesia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thermostable α-amylase from Geobacillus sp. DS3, isolated from the Sikidang Crater, Dieng Plateau, Indonesia, was previously purified and characterized. However, production from thermophilic bacteria requires high-temperature cultivation. This study aimed to clone and express the amy gene encoding α-amylase in Escherichia coli BL21(DE3) for easier enzyme production. The amy gene (1638 bp) was amplified via PCR, TA-cloned, and inserted into the pET-SUMO expression vector, which includes an N-terminal His-tag and SUMO-tag to enhance expression and solubility. The recombinant plasmid (pET-SUMO-amy) was transformed into E. coli BL21(DE3) for protein expression. Homology modelling using MOE software and template PDB ID 1HVX (91.5% identity) revealed a reliable 3D structure. Structural analysis showed altered calcium and sodium ion binding compared to the template, with calcium ions interacting with more residues. Docking studies revealed that maltotetraose binding is stabilized by five key residues: Asp268, His272, Trp300, Asn363, and Asp365. The enzyme displayed optimal activity at 70 °C and retained 60% activity at 90 °C. Kinetic parameters showed a low K

Indexed as

alpha-AmylasesBacterial ProteinsCloning, MolecularGeobacillusEnzyme StabilityEscherichia coliHot TemperatureKineticsModels, MolecularMolecular Docking SimulationRecombinant Proteinsalpha-AmylasesBacterial ProteinsRecombinant Proteins1HVXGeobacillus sp. DS3Molecular dockingRecombinantThermostable α-amylase

Identifiers

PMID40982022

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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.