Abstract
Chicken feathers are predominantly composed of keratin; hence, valorizing the wastes becomes an imperative. In view of this, we isolated keratinase-producing bacteria and identified them through the 16S rDNA sequence. The process condition for keratinase activity was optimized, and electron micrography of the degradation timelines was determined. Keratinolytic bacteria were isolated and identified as Bacillus sp. FPF-1, Chryseobacterium sp. FPF-8, Brevibacillus sp. Nnolim-K2, Brevibacillus sp. FPF-12 and Brevibacillus sp. FSS-1; and their respective nucleotide sequences were deposited in GenBank, with the accession numbers MG214993, MG214994, MG214995, MG214996 and MG214999. The degree of feather degradation and keratinase concentration among the isolates ranged from 62.5 ± 2.12 to 86.0 ± 1.41(%) and 214.55 ± 5.14 to 440.01 ± 20.57 (U/mL), respectively. In the same vein, 0.1% (w/v) xylose, 0.5% (w/v) chicken feather, an initial fermentation pH of 5.0, fermentation temperature of 25 °C and an agitation speed of 150 rpm, respectively, served as the optimal physicochemical conditions for keratinase activity by Bacillus sp. FPF-1. The time course showed that Bacillus sp. FPF-1 yielded a keratinase concentration of 1698.18 ± 53.99(U/mL) at 120 h. The electron microscopic imaging showed completely structural dismemberment of intact chicken feather. Bacillus sp. FPF-1 holds great potential in the valorization of recalcitrant keratinous biomass from the agro sector into useful products.
Highlights
Chicken feathers are a significant waste product from poultry processing farms, and the disposal process has remained incineration, commuting to landfills and limited use as non-nutritive additives of feed
The 16S rDNA nucleotide sequences basic local alignment search tool (BLAST) showed the isolate coded as FPF-1 to have a high sequence homology (100%) with Bacillus cereus AB1 (MF800922) and Bacillus thuringiensis WG20 (KY085971); the isolate was identified as Bacillus sp
The other isolates coded as FPF-10, FPF-12 and FSS-1 showed 99% sequence homology with Brevibacillus parabrevis C20 (KX832699), Brevibacillus parabrevis NAP3 (KJ872854) and Brevibacillus sp
Summary
Chicken feathers are a significant waste product from poultry processing farms, and the disposal process has remained incineration, commuting to landfills and limited use as non-nutritive additives of feed. The composition of chicken feathers includes keratin, which bestows the mechanical stability associated with chicken feathers, leading to the recalcitrance to degradation [1]. The estimated abundance of crude protein in the avian feather has been approximated to about 82.36% [2], and this significant protein content portends an excellent opportunity for the valorization of the agro-waste biomass to high-value, cost-effective and renewable-source proteins for various applications, including livestock-feed supplementation. Notwithstanding the potentials presented by avian feathers as a high-protein source, the ability to dismember the feathers into functional components becomes the key for the valorization of the agro-waste. The traditional approach for the valorization of feathers involves endergonic reactions and chemical treatments [3]; these methods are capital intensive, and they produce a poorly digestible protein which is unsatisfactory as a feed supplement. The application of the methods incorporates other compounds with no known biological importance [4]
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