ArticleCurrent microbiology2022
Aspergillus welwitschiae: A Potential amylases Producer.
Article in Current microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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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.
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.
Who cites it
2 citing papers in PubMed, 3 citations in OpenAlex.
- Aspergillus Welwitschiae Regulates Response of Wheat at Multiple Levels To Alleviate Induced Chromate Stress.Current microbiology · 2025Article
- Characterization of an α-Amylase from the Honeybee Chalk Brood PathogenJournal of fungi (Basel, Switzerland) · 2023Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amylases, glycoside hydrolases widely used in several industrial processes, can be produced by many animals, plants, bacteria, and fungi. Fungal amylases from Aspergillus sp. hold remarkable importance in biotechnological applications for presenting a great catalysis efficiency in a wide range of pH and temperature. The production of amylases is mainly dependent on the genetic background of the species, i.e., Aspergillus strains, and abiotic factors. Among the major producers of amylases are the species of Aspergillus section Nigri, including Aspergillus welwitschiae. In this study, Aspergillus welwitschiae strains were evaluated for their ability to produce extracellular amylases. Among the 24 strains, wild Aspergillus welwitschiae UELAs 15.262 and mutant A. welwitschiae UELAs 15.262/35 strains showed greater potential for amylases production. The A. welwitschiae UELAs 15.262 produced more amylases (8645 U/mg) when compared to A. welwitschiae UELAs 15.262/35 (6666 U/mg). The amylases activity from partially purified crude enzymatic extract of A. welwitschiae UELAs 15.262 strain obtained at pH 5.5, 60 °C, resulted in 1.98-fold (3837 U/mg) increase in enzymatic activity. Likewise, the amylases activity from partially purified crude extract of A. welwitschiae UELAs 15.262/35 obtained at pH 5.0, 60 °C resulted in 2.2-fold (9077 U/mg) increase in amylases activity. The presence of metallic ions (Cu
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Registered trials
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 Socratic graph.