ArticleMicrobial biotechnology2020
Identification of keratinases from Fervidobacterium islandicum AW-1 using dynamic gene expression profiling.
Article in Microbial biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 42 citations in OpenAlex.
- Integrated multiomics reveals starvation-driven keratin degradation and persistence iniScience · 2026Article
- Functional identification of a feather-degrading thermitase-like S8 serine protease fromFrontiers in microbiology · 2026Article
- Proteolytic and non-proteolytic mechanisms of keratin degradation inApplied and environmental microbiology · 2025Article
- Streptomyces shaoguanensis sp. nov.: elucidating the mechanisms of efficient chicken feather degradation and its potential for biofertilizer development.Microbial cell factories · 2025Article
- Diversity, metabolic potential and global distribution of the anaerobic fermentative bacteria Phylum Candidatus Cloacimonadota.Environmental microbiome · 2025Article
- Efficient Mining and Characterization of Two Novel Keratinases from Metagenomic Database.Biomolecules · 2025Article
- 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
- Transcriptomic and proteomic insights into feather keratin degradation byFrontiers in microbiology · 2025Article
- Isolation, Selection, and Identification of Keratinolytic Bacteria for Green Management of Keratin Waste.Molecules (Basel, Switzerland) · 2024Article
- High keratinase and other types of hydrolase activity of the new strain of Bacillus paralicheniformis.PloS one · 2024Article
- Hyperthermophile diversity microbes in the Calientes geothermal field, Tacna, Peru.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023Article
- Insights into the keratin efficient degradation mechanism mediated by Bacillus sp. CN2 based on integrating functional degradomics.Biotechnology for biofuels and bioproducts · 2023Article
- Hybrid De Novo Whole-Genome Assembly, Annotation, and Identification of Secondary Metabolite Gene Clusters in the Ex-Type Strain ofJournal of fungi (Basel, Switzerland) · 2023Article
- Genome-wide analysis of Keratinibaculum paraultunense strain KD-1Archives of microbiology · 2022Article
- Feather-Degrading Bacillus cereus HD1: Genomic Analysis and Its Optimization for Keratinase Production and Feather Degradation.Current microbiology · 2022Article
- Keratinases as Versatile Enzymatic Tools for Sustainable Development.Biomolecules · 2021Review
- The sulfur formation system mediating extracellular cysteine-cystine recycling in Fervidobacterium islandicum AW-1 is associated with keratin degradation.Microbial biotechnology · 2021Article
- Effect of Cultivation Parameters on Fermentation and Hydrogen Production in the PhylumInternational journal of molecular sciences · 2020Review
- Microbial enzymes catalyzing keratin degradation: Classification, structure, function.Biotechnology advances · 2020Review
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Keratin degradation is of great interest for converting agro-industrial waste into bioactive peptides and is directly relevant for understanding the pathogenesis of superficial infections caused by dermatophytes. However, the mechanism of this process remains unclear. Here, we obtained the complete genome sequence of a feather-degrading, extremely thermophilic bacterium, Fervidobacterium islandicum AW-1 and performed bioinformatics-based functional annotation. Reverse transcription PCR revealed that 57 putative protease-encoding genes were differentially expressed in substrate-dependent manners. Consequently, 16 candidate genes were highly expressed under starvation conditions, when keratin degradation begun. Subsequently, the dynamic expression profiles of these 16 selected genes in response to feathers, as determined via quantitative real-time PCR, suggested that they included four metalloproteases and two peptidases including an ATP-dependent serine protease, all of which might act as key players in feather decomposition. Furthermore, in vitro keratinolytic assays supported the notion that recombinant enzymes enhanced the decomposition of feathers in the presence of cell extracts. Therefore, our genome-based systematic and dynamic expression profiling demonstrated that these identified metalloproteases together with two additional peptidases might be primarily associated with the decomposition of native feathers, suggesting that keratin degradation can be achieved via non-canonical catalysis of several membrane-associated metalloproteases in cooperation with cytosolic proteases.
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