ReviewWorld journal of microbiology & biotechnology2023
Microbial glucoamylases: structural and functional properties and biotechnological uses.
Review in World journal of microbiology & biotechnology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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.
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
5 citing papers in PubMed, 15 citations in OpenAlex.
- Prenylated Isoflavones Originating from East African Medicinal Plants Selectively Modulate the α-Glucosidase fromJournal of natural products · 2026Article
- A Multienzyme Magnetic Nanocatalyst for Efficient, Sustainable Hydrolysis of Wastewater-Grown Microalgae Consortia.ACS sustainable chemistry & engineering · 2026Article
- Spatiotemporal Profiling of Starch-Degrading Enzymes in Nong-Flavor Daqu: Molecular Markers for Quantitative Quality Evaluation.Foods (Basel, Switzerland) · 2025Article
- Development of an efficient heterologous protein expression platform in Aspergillus niger through genetic modification of a glucoamylase hyperproducing industrial strain.Microbial cell factories · 2025Article
- Optimization of Enzymatic Hydrolysis and Fermentation Processing for Set-Type Oat Yogurt with Favorable Acidity and Coagulated Texture.Foods (Basel, Switzerland) · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Glucoamylases (GAs) are one of the principal groups of enzymes involved in starch hydrolysis and belong to the glycosylhydrolase family. They are classified as exo-amylases due to their ability to hydrolyze α-1,4 glycosidic bonds from the non-reducing end of starch, maltooligosaccharides, and related substrates, releasing β-D-glucose. Structurally, GAs possess a characteristic catalytic domain (CD) with an (α/α)
Indexed as
Identifiers
What OpenQuestion holds
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 OpenQuestion graph.