ArticleBMC biotechnology2020
Bacillus sp. CSK2 produced thermostable alkaline keratinase using agro-wastes: keratinolytic enzyme characterization.
Article in BMC biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 41 citations in OpenAlex.
- Multi-targeted synergy of Bacillus sp. TC5 fermentation products for transdermal drug delivery and hair regeneration.Journal of advanced research · 2026Article
- Biodegradation of hair waste for keratinase production using Bacillus altitudinis VK-1120 and its application in enzymatic dehairing.Biodegradation · 2026Article
- Keratinases: microbial sources, mechanisms, and industrial applications in waste valorization.Frontiers in microbiology · 2026Review
- Proteolytic enzymes from Bacillus subtilis AB2 as antibiofilm adjuvants: Bioprocess optimization, mechanistic insights, and synergy with antibiotics.Journal of microbiology (Seoul, Korea) · 2025Article
- Dietary RISCO NUTRIFOUR multistrain multikingdom probiotic consortia improves meat quality carcass traits and growth efficiency in heat stressed broilers.Scientific reports · 2025Article
- Feather Waste Biodegradation and Biostimulant Potential ofInternational journal of molecular sciences · 2025Article
- An update on thermostable keratinases for protein engineering against feather pollutants.Applied microbiology and biotechnology · 2025Review
- New Bacillus paralicheniformis strain with high proteolytic and keratinolytic activity.Scientific reports · 2024Article
- High keratinase and other types of hydrolase activity of the new strain of Bacillus paralicheniformis.PloS one · 2024Article
- Response surface methodology based optimization of keratinase fromSaudi journal of biological sciences · 2023Article
- Thermoactive metallo-keratinase fromHeliyon · 2023Article
- Biochemical and molecular characterization of novel keratinolytic protease fromFrontiers in microbiology · 2023Article
- Valorization of Livestock Keratin Waste: Application in Agricultural Fields.International journal of environmental research and public health · 2022Review
- 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
- Understanding the Basis of Occurrence, Biosynthesis, and Implications of Thermostable Alkaline Proteases.Applied biochemistry and biotechnology · 2021Review
- The keratinolytic bacteria Bacillus cytotoxicus as a source of novel proteases and feather protein hydrolysates with antioxidant activities.Journal, genetic engineering & biotechnology · 2021Article
- Novel recombinant keratin degrading subtilisin like serine alkaline protease from Bacillus cereus isolated from marine hydrothermal vent crabs.Scientific reports · 2021Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundChicken feathers are the most abundant agro-wastes emanating from the poultry processing farms and present major concerns to environmentalists. Bioutilization of intractable feather wastes for the production of critical proteolytic enzymes is highly attractive from both ecological and biotechnological perspectives. Consequently, physicochemical conditions influencing keratinase production by Bacillus sp. CSK2 on chicken feathers formulation was optimized, and the keratinase was characterized.
resultsThe highest enzyme activity of 1539.09 ± 68.14 U/mL was obtained after 48 h of incubation with optimized conditions consisting of chicken feathers (7.5 g/L), maltose (2.0 g/L), initial fermentation pH (5.0), incubation temperature (30 °C), and agitation speed (200 rpm). The keratinase showed optimal catalytic efficiency at pH 8.0 and a temperature range of 60 °C - 80 °C. The keratinase thermostability was remarkable with a half-life of above 120 min at 70 °C. Keratinase catalytic efficiency was halted by ethylenediaminetetraacetic acid and 1,10-phenanthroline. However, keratinase activity was enhanced by 2-mercaptoethanol, dimethyl sulfoxide, tween-80, but was strongly inhibited by Al
conclusionThe remarkable stability of the keratinase with an admixture of organic solvents or laundry detergents portends the industrial and biotechnological significance of the biocatalyst.
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