ArticleAMB Express2020
Recombinant expression and biochemical characterization of a novel keratinase BsKER71 from feather degrading bacterium Bacillus subtilis S1-4.
Article in AMB Express, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 37 citations in OpenAlex.
- A Highly Active Keratinase fromBiomolecules · 2025Article
- Current Understanding of Feather Keratin and Keratinase and Their Applications in Biotechnology.Biochemistry research international · 2025Review
- Unlocking the Keratinolytic Potential ofProtein and peptide letters · 2025Article
- The flexible linker and CotG were more effective for the spore surface display of keratinase KERQ7.World journal of microbiology & biotechnology · 2023Article
- Synthesis and characterization of keratinase laden green synthesized silver nanoparticles for valorization of feather keratin.Scientific reports · 2023Article
- Dynamics of the Bacterial Community's Soil During the In-Situ Degradation Process of Waste Chicken Feathers.Indian journal of microbiology · 2022Article
- Feather-Degrading Bacillus cereus HD1: Genomic Analysis and Its Optimization for Keratinase Production and Feather Degradation.Current microbiology · 2022Article
- Directed evolution driving the generation of an efficient keratinase variant to facilitate the feather degradation.Bioresources and bioprocessing · 2022Article
- Chicken Feather Waste Valorization Into Nutritive Protein Hydrolysate: Role of Novel Thermostable Keratinase FromFrontiers in microbiology · 2022Article
- Perspectives on Converting Keratin-Containing Wastes Into Biofertilizers for Sustainable Agriculture.Frontiers in microbiology · 2022Review
- Keratinases as Versatile Enzymatic Tools for Sustainable Development.Biomolecules · 2021Review
- Structure, Application, and Biochemistry of Microbial Keratinases.Frontiers in microbiology · 2021Review
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
Bacillus subtilis S1-4, isolated from chicken feather could efficiently degrade feathers by secreting several extracellular proteases. In order to get insight into the individual protease involved in keratin hydrolysis, a keratinase designed as BsKER71 was cloned and expressed in Bacillus subtilis WB600. In silico analysis revealed that BsKER71 protein contained a mature protein of 36.1 kDa. Further, purified BsKER71 could hydrolyze a variety of natural proteins, such as fibrous protein, collagen protein, casein, keratin and bovine serum albumin. In addition, this keratinase exhibited high enzyme activity in a wide range of pH and optimal pH of 10.0 and 9.0 in the hydrolysis of casein and keratin, respectively. Similarly, the optimal temperature was 55 °C and 50 °C for the hydrolysis of above two substrates, respectively. The hydrolytic activity was significantly inhibited by phenylmethanesulfonyl fluoride (PMSF), indicating the presence of serine residue in the active site. Moreover, ethylenediaminetetraacetic acid (EDTA) and phenanthroline moderately inhibited the hydrolytic activity. The catalytic activity was stimulated by Mg
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