ArticleCurrent microbiology2023
Bacillus Swezeyi B2 Strain: A Novel Alkaliphilic Bacterium Producer of Alkaline-, Thermal, Oxidant-, and Surfactant-Stable Protease, Extremely Efficient in Detergency.
Article in Current microbiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
3 citing papers in PubMed, 11 citations in OpenAlex.
- Microbial Proteases: Integration into Food Products and Industrial Processes.Current microbiology · 2025Review
- Advances in Microbial Alkaline Proteases: Addressing Industrial Bottlenecks Through Genetic and Enzyme Engineering.Applied biochemistry and biotechnology · 2025Review
- Strawberry Protease as a Laundry Detergent Additive Candidate: Immobilization, Compatibility Study with Detergent Ingredients, and Washing Performance Test.Global challenges (Hoboken, NJ) · 2024Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteolytic enzymes that are currently used to meet industrial demand are usually derived from Bacillus species. They find multiple technical applications, particularly they have been increasingly used as a key bio-additive in detergents. In this study, a novel alkalophilic bacterium was isolated from contaminated soil, exhibiting 1400 U/ml proteolytic activity, and identified as Bacillus swezeyi B2. The crude enzyme likely contained a single extracellular protease. This enzyme revealed optimum activity at pH 10 and 70 °C and was highly alkaline thermostable (7-12.5) and up to 70 °C. The protease activity was completely inhibited by Phenylmethylsulfonyl fluoride (PMSF) suggesting that it belongs to the serine protease group. It was highly stable in the presence of the strong anionic surfactant (SDS) and oxidizing agents (H
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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.