Isolation, identification, and characterization of a feather-degrading bacterium.
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A feather-degrading culture was enriched with isolates from a poultry waste digestor and adapted to grow with feathers as its primary source of carbon, sulfur, and energy, indicating a potential biotechnique for degradation and utilization of feather keratin.Abstract:
A feather-degrading culture was enriched with isolates from a poultry waste digestor and adapted to grow with feathers as its primary source of carbon, sulfur, and energy. Subsequently, a feather-hydrolytic, endospore-forming, motile, rod-shaped bacterium was isolated from the feather-degrading culture. The organism was Gram stain variable and catalase positive and demonstrated facultative growth at thermophilic temperatures. The optimum rate of growth in nutrient broth occurred at 45 to 50°C and at pH 7.5. Electron microscopy of the isolate showed internal crystals. The microorganism was identified as Bacillus licheniformis PWD-1. Growth on hammer-milled-feather medium of various substrate concentrations was determined by plate colony count. Maximum growth (approximately 109 cells per ml) at 50°C occurred 5 days postinoculation on 1% feather substrate. Feather hydrolysis was evidenced as free amino acids produced in the medium. The most efficient conditions for feather fermentation occurred during the incubation of 1 part feathers to 2 parts B. licheniformis PWD-1 culture (107 cells per ml) for 6 days at 50°C. These data indicate a potential biotechnique for degradation and utilization of feather keratin.read more
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Characterization of a keratinolytic serine protease from Bacillus subtilis KS-1.
Hyung Joo Suh,Hyo Ku Lee +1 more
TL;DR: A keratinolytic enzyme produced by Bacillus subtilis KS-1 isolated from poultry waste was purified and characterized using ultrfiltration, DEAE-Sephadex, and SephadeX G-100 chromatographies, which suggest that the cleavage of the disulfide bonds with reducing agents can occur directly or by excretion of sulfite, which causes the sulfitolysis of the Disulfide Bonds.
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Revisiting microbial keratinases: next generation proteases for sustainable biotechnology.
TL;DR: A comprehensive review on microbial keratinases is presented giving an account of chronological progress of research along with the major milestones, and major focus has been on the key characteristics of keratinase, such as substrate specificity, keratin degradation mechanisms, molecular properties, and their role in prion decontamination along with other pharmaceutical applications.
Journal ArticleDOI
Keratinolytic activity of Bacillus megaterium F7-1, a feather-degrading mesophilic bacterium
Geuntae Park,Hong-Joo Son +1 more
TL;DR: B. megaterium F7-1 presented high keratinolytic activity and was very effective in feather degradation, providing potential use for biotechnological processes of keratin hydrolysis.
Journal ArticleDOI
Fermentation production of keratinase from Bacillus licheniformisPWD-1 and a recombinant B. subtilis FDB-29.
J.-J. Wang,Jason C. H. Shih +1 more
TL;DR: After respective optimization of fermentation conditions, keratinase production by B. licheniformis PWD-1 is approximately 40% higher than thatBy B. subtilis FDB-29, a recombinant strain, and control of pH is not necessary.
Journal ArticleDOI
Hide depilation and feather disintegration studies with keratinolytic serine protease from a novel Bacillus subtilis isolate
Priya Pillai,G. Archana +1 more
TL;DR: A single major PMSF-sensitive protease band could be detected upon zymogram analysis, indicating that a single enzyme may be responsible for feather degradation and hide depilation.
References
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Effects of processing time and moisture content on amino acid composition and nitrogen characteristics of feather meal
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Keratin as a source of protein for the growing chick. 1. Amino acid imbalance as the cause for inferior performance of feather meal and the implication of disulfide bonding in raw feathers as the reason for poor digestibility.
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