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ARTICLE; AGRICULTURE AND ENVIRONMENTAL BIOTECHNOLOGY Bacillus safensis LAU 13: a new source of keratinase and its multi-functional biocatalytic applications

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TLDR
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.
Abstract
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. The wild-type strain produced 35.450.4 U/mL keratinase over a period of 120 h, while the mutant one yielded 64.4108.5 U/mL keratinase for the same period of 120 h. The optimal conditions for the enzyme activities were pH 7.5 and 40 C. The mutant and wild-type strain keratinases retained 59% and 54% of their activity after 12 h pretreatment at 40 C, and 64% and 60% of their activity after 12 h at pH 7.5, respectively. The keratinases showed high substrate specificity for feathers, but low specificity for human and bovine hairs. The enzymes were activated by Na C ,C a 2C ,F e 2C and Mg 2C . However, while Mn 2C activated the enzyme from the mutant strain, it inhibited that of the wild type. The mutant and wild-type strain completely degraded whole chicken feathers after 6 and 9 days at 30 § 2 C, and also completely dehaired goat skin within 12 and 16 h, respectively, without damage to the skin. Similarly, remarkable destaining of blood-stained cloth occurred within 23 h. The obtained results showed an improvement in the properties of the mutant strain for use of the microorganism or its enzyme as biocatalysts.

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A novel approach to the green synthesis of metallic nanoparticles: the use of agro-wastes, enzymes, and pigments

I. A. Adelere, +1 more
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Green synthesis of silver nanoparticles using keratinase obtained from a strain of Bacillus safensis LAU 13

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References
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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

Purification and characterization of an extracellular alkaline serine protease with dehairing function from Bacillus pumilus.

TL;DR: An extracellular alkaline serine protease (called DHAP), produced by a Bacillus pumilus strain, demonstrates significant dehairing function and is purified by hydrophobic interaction chromatography, ion exchange, and gel filtration.
Journal ArticleDOI

Keratinolytic potential of Bacillus licheniformis RG1: structural and biochemical mechanism of feather degradation

TL;DR: Scanning electron microscopy studies revealed that bacterial cells grew closely adhered to the barbules of feathers, completely degrading them within 24 h, emphasizing that bacterial adhesion plays a key role during the degradation process.
Journal ArticleDOI

Keratinase production and keratin degradation by a mutant strain of Bacillus subtilis

TL;DR: Strain KD-N2 shows great promise of finding potential applications in keratin hydrolysis and keratinase production and screened for mutants with elevated keratinolytic activity using N-methyl-N′-nitro-N-nitrosoguanidine mutagenesis.
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.
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