ArticleInternational journal of biochemistry and molecular biology2023
Periplasmic β-glucosidase BglX from
Article in International journal of biochemistry and molecular biology, 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, 3 citations in OpenAlex.
- Clinically relevant genomic and phenotypic differences in virulence, antimicrobial resistance, and biofilm-associated tolerance between Streptococcus suis lineages ST1 and ST123.Veterinary research · 2026Article
- Lactulose-Induced Transcriptional Reprogramming and Repression of Persistence-Associated Phenotypes in Non-TyphoidalPathogens (Basel, Switzerland) · 2026Article
- Amygdalin-Doped Biopolymer Composites as Potential Wound Dressing Films: In Vitro Study onGels (Basel, Switzerland) · 2025Article
- Comprehensive analysis of orthologous genes reveals functional dynamics and energy metabolism in the rhizospheric microbiome of Moringa oleifera.Functional & integrative genomics · 2025Article
- Effect of Glycosidase Production byFoods (Basel, Switzerland) · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe diverse nature of carbohydrate structures and linkages requires a variety of enzymes responsible for sugar degradation. The
objectivesWe investigated the catalytic properties of the
methodsThe
resultsSubstrate specificity tests indicated that the BglX enzyme hydrolyzes β-glycosidic bonds in nitrophenyl-β-glycosides and demonstrates greater activity towards galactose-containing substrates compared to glucose derivatives. Monomeric glucose and galactose inhibit enzyme activity to a different degree in a substrate-dependent manner. In addition, BglX can hydrolyze lactose but not cellobiose, maltose, or laminarin. Subsequently,
conclusionsThe low activity towards glucose-containing substrates and significantly elevated activity towards galactosides suggests that β-glucosidase activity may not be the primary function of the BglX enzyme.
Indexed as
Identifiers
37736388PMC10509532W4386944856What 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.