Isolation and characterization of a new keratinolytic bacterium that exhibits significant feather-degrading capability
TLDR
Potential biotechnological applications of this bacterium that involve hydrolysis of keratin, including the improvement of the nutritional properties of feathers (and other keratins) used as supplementary feedstuffs are suggested.Abstract:
A novel bacterium, Bacillus licheniformis K-19, which produces a large amount of akeratinase that is extremely thermostable and has a broad resistance to pH, was isolated and characterized. The maximum amount of keratinase activity (about 224 Uml-1) was produced at 37°C when the bacterium was cultured for 72 h in broth containing feather meal with initial pH of 7.5. The keratinase activity was observed over a wide range of temperatures (30 - 90°C) and pH values (pH 6 - 10). It was optimal at 60°C and pH 7.5 - 8 respectively. These results suggest potential biotechnological applications of this bacterium that involve hydrolysis of keratin, including the improvement of the nutritional properties of feathers (and other keratins) used as supplementary feedstuffs.
Key words: Bacillus licheniformis, chicken feather, keratin, keratinolytic protease.read more
Citations
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Journal ArticleDOI
Bacillus safensis LAU 13: a new source of keratinase and its multi-functional biocatalytic applications
TL;DR: A newly isolated bacterium identified as Bacillus safensis based on biochemical tests and 16S rRNA analysis and its mutant variant created by exposure to ultraviolet radiation at 254 nm were investigated for keratinolytic activity as mentioned in this paper.
ARTICLE; AGRICULTURE AND ENVIRONMENTAL BIOTECHNOLOGY Bacillus safensis LAU 13: a new source of keratinase and its multi-functional biocatalytic applications
TL;DR: The obtained results showed an improvement in the properties of the mutant strain for use of the micro-organism or its enzyme as biocatalysts and high substrate specificity for feathers, but low specificity for human and bovine hairs.
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Keratinase production and biodegradation of whole chicken feather keratin by a newly isolated bacterium under submerged fermentation.
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TL;DR: The manuscript first time describes B. weihenstephanensis PKD 5-mediated keratinase production under submerged fermentation and whole chicken feather biodegradation.
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Microbial keratinases: An overview of biochemical characterization and its eco-friendly approach for industrial applications
TL;DR: Keratin is resistant to degradation by common proteases and chemical catalysts due to high mechanical stability and cross-linked disulphide bonds present in their structure as mentioned in this paper.
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Transforming Chicken Feather Waste into Feather Protein Hydrolysate Using a Newly Isolated Multifaceted Keratinolytic Bacterium Chryseobacterium sediminis RCM-SSR-7
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References
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Journal ArticleDOI
Purification and Characterization of a Keratinase from a Feather-Degrading Bacillus licheniformis Strain
TL;DR: The purified keratinase hydrolyzes a broad range of substrates and displays higher proteolytic activity than most proteases and is a useful enzyme for promoting the hydrolysis of feather keratin and improving the digestibility of feather meal.
Journal ArticleDOI
Isolation, identification, and characterization of a feather-degrading bacterium.
TL;DR: 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.
Journal Article
The use of azoalbumin as a substrate in the colorimetric determination or peptic and tryptic activity.
Journal ArticleDOI
Characterization of a new keratinolytic bacterium that completely degrades native feather keratin.
TL;DR: A novel feather-degrading microorganism was isolated from poultry waste, producing a high keratinolytic activity when cultured on broth containing native feather, and complete feather degradation was achieved during cultivation.
Journal ArticleDOI
Native-feather degradation by Fervidobacterium islandicum AW-1, a newly isolated keratinase-producing thermophilic anaerobe
Gae Won Nam,Dong Woo Lee,Han Seoung Lee,Nam Lee,Byoung-Chan Kim,Eun Ah Choe,Jae Kwan Hwang,Maggy Thenawidjaja Suhartono,Yu Ryang Pyun +8 more
TL;DR: The enzyme from F. islandicum AW-1 is a novel, thermostable keratinolytic serine protease that showed higher specific activity for the keratinous substrates than other proteases and catalyzed the cleavage of peptide bonds more rapidly following the reduction of disulfide bridges in feather keratin by 10 mM dithiothreitol.
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