ArticleWorld journal of microbiology & biotechnology2019
Cloning and expression of a thermostable keratinase gene from Thermoactinomyces sp. YT06 in Escherichia coli and characterization of purified recombinant enzymes.
Article in World journal of microbiology & biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 27 citations in OpenAlex.
- Production, biochemical characterization, and kinetic/thermodynamic analysis of a novel keratinase from Bacillus sp. MSGU2024.Biotechnology letters · 2026Article
- Keratinases: microbial sources, mechanisms, and industrial applications in waste valorization.Frontiers in microbiology · 2026Review
- An update on thermostable keratinases for protein engineering against feather pollutants.Applied microbiology and biotechnology · 2025Review
- 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
- High keratinase and other types of hydrolase activity of the new strain of Bacillus paralicheniformis.PloS one · 2024Article
- Structure prediction, docking studies and molecular cloning of novel Pichia kudriavzevii YK46 metalloprotease (MetPr) for improvement of feather waste biodegradation.Scientific reports · 2023Article
- Microbial Pretreatment of Chicken Feather and Its Co-digestion With Rice Husk and Green Grocery Waste for Enhanced Biogas Production.Frontiers in microbiology · 2022Article
- A Newly Isolated StrainFrontiers in microbiology · 2022Article
- High level expression and biochemical characterization of an alkaline serine protease from Geobacillus stearothermophilus to prepare antihypertensive whey protein hydrolysate.BMC biotechnology · 2021Article
- Extracellular Production, Characterization, and Engineering of a Polyextremotolerant Subtilisin-Like Protease From Feather-DegradingFrontiers in microbiology · 2020Article
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Authors and funding
6 authors at 2 institutions in 1 country.
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Abstract
The feather-degrading strain Thermoactinomyces sp. YT06 secretes an extracellular keratinolytic protease (KERTYT); however, the gene encoding this protease remains unknown. The kerT1 gene (1170 bp) encoding keratinase was cloned and expressed in Escherichia coli BL21(DE3). Purified recombinant keratinase (rKERTYT) was achieved at a yield of 39.16% and 65.27-fold purification with a specific activity of 1325 U/mg. It was shown that rKERTYT has many similarities to the native enzyme (KERTYT) by characterization of rKERTYT. The molecular weight of rKERTYT secreted by recombinant E. coli was approximately 28 kDa. The optimal temperature and the pH values of rKERTYT were 65 °C and 8.5, respectively, and the protein remained stable from 50 to 60 °C and pH 6-11. The keratinase was strongly inhibited by phenyl methane sulfonyl fluoride (PMSF), suggesting that it belongs to the serine protease family. It was significantly activated by Mn
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