Evidence map›Paper›PMID 33706728›Full record

ArticleBMC biotechnology2021

High level expression and biochemical characterization of an alkaline serine protease from Geobacillus stearothermophilus to prepare antihypertensive whey protein hydrolysate.

Chang Chang, Siyi Gong, Zhiping Liu, Qiaojuan Yan, Zhengqiang Jiang

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in BMC biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.1field-weighted citation impact, top 23% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

11 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Thermostable Proteases fromMicroorganisms · 2025
    Review
  5. Article
  6. Foods (Basel, Switzerland) · 2025
    Review
  7. Article
  8. Microbial proteases and their applications.Frontiers in microbiology · 2023
    Review
  9. High-expression and characterization of a novel serine protease from Ornithinibacillus caprae L9Environmental science and pollution research international · 2022
    Article
  10. Overexpression ofFrontiers in microbiology · 2022
    Article
  11. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Chang ChangKey Laboratory of Food Bioengineering (China National Light Industry), College of Food Science and Nutritional Engineering, China Agricultural University, No. 17 Qinghua Donglu, Beijing, 100083, China.
Siyi GongKey Laboratory of Food Bioengineering (China National Light Industry), College of Food Science and Nutritional Engineering, China Agricultural University, No. 17 Qinghua Donglu, Beijing, 100083, China.
Zhiping LiuKey Laboratory of Food Bioengineering (China National Light Industry), College of Food Science and Nutritional Engineering, China Agricultural University, No. 17 Qinghua Donglu, Beijing, 100083, China.
Qiaojuan YanBeijing Advanced Innovation Center for Food Nutrition and Human Health, College of Engineering, China Agricultural University, Beijing, 100083, China.
Zhengqiang JiangKey Laboratory of Food Bioengineering (China National Light Industry), College of Food Science and Nutritional Engineering, China Agricultural University, No. 17 Qinghua Donglu, Beijing, 100083, China. zhqjiang@cau.edu.cn.
China Agricultural University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundProteases are important for hydrolysis of proteins to generate peptides with many bioactivities. Thus, the development of novel proteases with high activities is meaningful to discover bioactive peptides. Because natural isolation from animal, plant and microbial sources is impractical to produce large quantities of proteases, gene cloning and expression of target protease are preferred.

resultsIn this study, an alkaline serine protease gene (GsProS8) from Geobacillus stearothermophilus was successfully cloned and expressed in Bacillus subtilis. The recombinant GsProS8 was produced with high protease activity of 3807 U/mL after high cell density fermentation. GsProS8 was then purified through ammonium sulfate precipitation and a two-step chromatographic method to obtain the homogeneous protease. The molecular mass of GsProS8 was estimated to be 27.2 kDa by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and 28.3 kDa by gel filtration. The optimal activity of GsProS8 was found to be pH 8.5 and 50 °C, respectively. The protease exhibited a broad substrate specificity and different kinetic parameters to casein and whey protein. Furthermore, the hydrolysis of whey protein using GsProS8 resulted in a large amount of peptides with high angiotensin-I-converting enzyme (ACE) inhibitory activity (IC

conclusionsGsProS8 could be a potential candidate for industrial applications, especially the preparation of antihypertensive peptides.

Indexed as

AnimalsAntihypertensive AgentsBacillus subtilisBacterial ProteinsBiocatalysisCattleCloning, MolecularEndopeptidasesEnzyme StabilityGeobacillus stearothermophilusHydrogen-Ion ConcentrationHydrolysisKineticsProtein HydrolysatesRecombinant ProteinsSerine Proteasesalkaline proteaseAntihypertensive AgentsBacterial ProteinsEndopeptidasesProtein HydrolysatesRecombinant ProteinsSerine ProteasesACE inhibitory activityAlkaline serine proteaseBacillus subtilisGeobacillus stearothermophilusWhey protein hydrolysate

Identifiers

PMID33706728
PMCPMC7953746
OpenAlexW3134344604

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.