ArticleProbiotics and antimicrobial proteins2018
Significant Hydrolysis of Wheat Gliadin by Bacillus tequilensis (10bT/HQ223107): a Pilot Study.
Article in Probiotics and antimicrobial proteins, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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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.
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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.
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Who cites it
5 citing papers in PubMed, 14 citations in OpenAlex.
- Optimizing Gluten Extraction Using Eco-friendly Imidazolium-Based Ionic Liquids: Exploring the Impact of Cation Side Chains and Anions.ACS omega · 2024Article
- Screening of Spore-Forming Bacteria with Probiotic Potential in Pristine Algerian Caves.Microbiology spectrum · 2022Article
- Celiac Disease and Possible Dietary Interventions: From Enzymes and Probiotics to Postbiotics and Viruses.International journal of molecular sciences · 2022Review
- Characterization ofFoods (Basel, Switzerland) · 2021Article
- New Insights into Non-Dietary Treatment in Celiac Disease: Emerging Therapeutic Options.Nutrients · 2021Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Peptidase therapy is suggested to be effective to minimize gliadin toxicity in celiac disease (CD). Hence, present study deals with gliadin-hydrolysing peptidases. The efficient peptidase from the Bacillus tequilensis was purified using ammonium sulfate fractionation and preparative electrophoresis. Analysis of in-solution and in-gel hydrolysis of gliadin using one and two-dimensional SDS-PAGE revealed nearly complete hydrolysis of gliadin peptides after 180 min of incubation with B. tequilensis protease. Purified peptidase was found to be stable at acidic (pH 3.5) to neutral (pH 7.2) pH range. The molecular mass and isoelectric point of the peptidase were observed around 29 kDa and 5.2, respectively. The internal protein sequence obtained through mass spectrometric analysis suggested that peptidase might belong to peptidase S9 family known for prolyl-specific peptidases. This study recommends the possible applicability of this peptidase for elimination of immunotoxic gliadin peptides and may prove useful in CD treatment.
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Registered trials
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