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Open AccessJournal ArticleDOI

Isolation and characterization of a new keratinolytic bacterium that exhibits significant feather-degrading capability

Bo Xu, +4 more
- 15 Sep 2009 - 
- Vol. 8, Iss: 18, pp 4590-4596
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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.

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Citations
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Journal ArticleDOI

Some applications of thermophiles and their enzymes for protein processing

TL;DR: This review covers thermostabilization strategies and some properties of thermostable proteases as well as their current and future applications in food processing, medicine and some other industries.
Journal Article

Biochemical and Molecular Characterization of Microbial Keratinase and Its Remarkable Applications

TL;DR: The bioconversion of insoluble feather keratin to soluble feather residue has high nutritional values and can be employed as a supplement for livestock feeds and other promising applications have been associated with keratinolytic enzymes.

Isolation, Partial purification and Characterization of Keratinase from Bacillus megaterium

TL;DR: The isolated strain of keratinase-producing bacterium was thermotolerant and alkalophilic bacterium which can therefore be used in leather processing and detergent industry and did not inhibit the enzyme.
Journal ArticleDOI

Keratinolytic activities of alkaliphilic Bacillus sp. MBRL 575 from a novel habitat, limestone deposit site in Manipur, India

TL;DR: Citrate and soybean meal were found to be the best carbon and nitrogen supplements for enhanced enzyme, soluble peptide and amino acid production and a promising isolate, MBRL 575, was found to degrade native chicken feather efficiently.
Journal ArticleDOI

Identification and characterization of feather-degrading bacteria from keratin-rich wastes

TL;DR: The thermostability of this enzyme makes it feasible to take advantage of this bacterium in biotechnological processes, and the highest keratinolytic activity exhibited in this strain was selected for further characterization.
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 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

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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