ArticleCurrent microbiology2021
Optimizing Protein-Glutaminase Expression in Bacillus subtilis.
Article in Current microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed, 37 citations in OpenAlex.
- Construction of an industrial host for the efficient active expression of protein glutaminase (PG) in Bacillus licheniformis.Bioprocess and biosystems engineering · 2026Article
- Enzymatic Deamidation of Plant Proteins by Protein-Glutamine Glutaminases: Effects on Solubility, Foaming and Emulsion Properties.Foods (Basel, Switzerland) · 2026Article
- Secretory Production of Mature Protein-Glutaminase from Bacteroides helcogenes in Bacillus subtilis.Applied biochemistry and biotechnology · 2026Article
- Toward food-grade production of the Bacteroides helcogenes protein-glutamine glutaminase with an optimized Bacillus subtilis strain.Applied microbiology and biotechnology · 2026Article
- Impact of expression systems on the transcriptome ofApplied and environmental microbiology · 2025Article
- L-glutaminase synthesis by Klebsiella pneumoniae (AS KP 23) isolated from clinical strain, and its efficacy against human hepatocellular and breast cancer cell lines.BMC microbiology · 2025Article
- Purified protein glutaminase fromFood chemistry: X · 2024Article
- An Efficient Prephenate Dehydrogenase Gene for the Biosynthesis of L-tyrosine: Gene Mining, Sequence Analysis, and Expression Optimization.Foods (Basel, Switzerland) · 2023Article
- L-Glutamine-, peptidyl- and protein-glutaminases: structural features and applications in the food industry.World journal of microbiology & biotechnology · 2022Review
- Genetic engineering for enhanced production of a novel alkaline protease BSP-1 inFrontiers in bioengineering and biotechnology · 2022Article
- The characteristics of protein-glutaminase from an isolatedFrontiers in microbiology · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein-glutaminase (PG) is a promising protein deaminase. It only hydrolyzes the side chain amido groups of protein-bound to generate ammonia and protein-L-glutamic acid and does not catalyze any other undesirable changes in protein structures. Deamidation of proteins via PG can influence the solubility, emulsification, foaming, and gelation properties of proteins, which are important properties for some food proteins. Therefore, there is great potential for the application of PG in the food industry. PG is derived from Chryseobacterium proteolyticum (C. proteolyticum); however, wild strains are difficult to industrialize because of their low levels of enzyme production. In this article, we studied different strategies for PG expression in B. subtilis. Results showed that PG produced from C. proteolyticum could be successfully secreted in B. subtilis WB800N, and actively secreted in B. subtilis 168(BS168) or DB403 containing a pro-peptide (pro-PG). The secreted PG from B. subtilis WB800N was inactive unless digested by exogenous proteases, such as trypsin, alkaline protease, and neutral protease. However, active PG was secreted by the self-processing of BS168 and DB403. The specific activity of purified PG reached 20.9 U/mg. PG showed maximum activity at pH 5.5, 55 °C and more than 80% of PG activity was retained within a range of pH 3.5-6.5. When Cbz-Gln-Gly was used as the substrate, PG activity was 31.1 ± 0.9 μM min
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.