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.
Dipak Kumar Sahoo,Arpan Das,Hrudayanath Thatoi,Keshab Chandra Mondal,Pradeep Kumar Das Mohapatra +4 more
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
Pintubala Kshetri,S. S. Roy,Susheel Kumar Sharma,Thangjam Surchandra Singh,Meraj Alam Ansari,Narendra Prakash,S. V. Ngachan +6 more
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
Feather keratin hydrolysis by a Vibrio sp. strain kr2
S. Sangali,Adriano Brandelli +1 more
TL;DR: Strain kr2 shows potential for use for biotechnological processes involving keratin hydrolysis, presenting similarities with that reported for feather lysate, feather meal and raw feathers.
Journal ArticleDOI
Production and characterization of keratinase of a feather-degrading Bacillus licheniformis PWD-1
TL;DR: The keratinase produced by Bacillus licheniformis PWD-1 was induced by feather powder and was stable from pH 5 to 12.5, and the relative activity of this enzyme toward casein, feather powder, keratin, elastin, and collagen was 100:52:41:18:7.
Journal ArticleDOI
Nucleotide sequence and expression of kerA, the gene encoding a keratinolytic protease of Bacillus licheniformis PWD-1
TL;DR: NorthernRNA analysis demonstrates that transcriptional regulation controls kerA expression on different growth media and deduced amino acid sequences indicate only three amino acid differences between the two mature proteases.
Journal ArticleDOI
Feather degradation by Bacillus sp. FK 46 in submerged cultivation
TL;DR: In this paper, the degradation of chicken feathers by Bacillus sp. FK 46 was investigated and the results showed that feather was almost completely degraded under the following conditions: 1% whole chicken feather as a substrate at the initial medium pH of 9 with 5% bacterial inoculum, at a temperature of 37 degrees C and a shaking speed of 250 rev/min.
Journal ArticleDOI
Isolation of Thermoanaerobacter keratinophilus sp. nov., a novel thermophilic, anaerobic bacterium with keratinolytic activity.
TL;DR: This strain, which grows optimally at 70°C, pH 7.0, and 0.5% NaCl, is the first member of the genus Thermoanaerobacter that has been described for its ability to degrade native keratin, and it is shown to possess intracellular and extracellular proteases optimally active.
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