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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

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.
Journal ArticleDOI

Keratinase production and biodegradation of whole chicken feather keratin by a newly isolated bacterium under submerged fermentation.

TL;DR: The manuscript first time describes B. weihenstephanensis PKD 5-mediated keratinase production under submerged fermentation and whole chicken feather biodegradation.
Journal ArticleDOI

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.
Journal ArticleDOI

Transforming Chicken Feather Waste into Feather Protein Hydrolysate Using a Newly Isolated Multifaceted Keratinolytic Bacterium Chryseobacterium sediminis RCM-SSR-7

TL;DR: This study revealed that FPH produced by C. sediminis RCM-SSR-7 has the potential to be used as animal feed and organic fertilizer and exhibited radical scavenging activity with an IC50 value of 0.102 mg ml−1.
References
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Journal ArticleDOI

Isolation, identification and characterization of a feather degrading bacterium.

TL;DR: Keratinases which are produced by these keratinolytic organisms could be used to degrade feather waste and further the digested products could be an excellent material for producing animal feed, fertilizers or natural gas.
Journal ArticleDOI

Isolation and characterization of a new keratinolytic Bacillus licheniformis strain

TL;DR: A keratin-degrading bacterium strain was isolated from partially degraded feathers and characterized and was identified as Bacillus licheniformis, which exhibited a high chicken feather-degRading activity when cultured in feather-containing broth with a growth optimum of pH 7.0.
Journal ArticleDOI

Secretion of a trypsin-like thiol protease by a new keratinolytic strain of Bacillus licheniformis.

TL;DR: When cultured in feather-containing broth with a growth optimum of pH 7.0 and 47 degrees C, a Bacillus licheniformis strain exhibited a high chicken feather-degrading activity and a trypsin-like protease was isolated from its ferment broth and was partially characterized.
Journal ArticleDOI

Selection and characterization of feather-degrading bacteria from canola meal compost.

TL;DR: Protease inhibition studies indicated that serine proteases are the predominant proteolytic enzymes produced by these feather-degrading isolates.
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