Hydrolyzing Proficiency of Keratinases in Feather Degradation

Gupta, Sonali; Singh, Rajni

doi:10.1007/s12088-014-0477-5

Cited by 42 publications

(31 citation statements)

References 20 publications

(18 reference statements)

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“…Several organic materials from animal origin, such as blood meal, hooves, horns, feathers, bones and manure have been evaluated as potential fertilizers [82]. [22] Chryseobacterium sediminis (µg) [72] Bacillus subtilis RSE163 (µM) [12] Bacillus subtilis RSE165 (µM) [ The use of feather hydrolyzate and keratinolytic bacteria having antagonistic and PGP activities could offer a number of economic and environmental advantages over chemicalbased as better organic fertilizer, biocontrol and biofertilizing agents. Organic amendments of N and/C rich feather hydrolyzate can serve the dual purpose of improving plant growth and stimulating beneficial microbial activity in soil.…”

Section: Discussionmentioning

confidence: 99%

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Feather degradation by keratinolytic bacteria and biofertilizing potential for sustainable agricultural production

et al. 2018

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Feathers account for 5–7% of the total weight of chicken have become one of the major pollutants due to their recalcitrant nature. Feather which is constituted of 90% keratin can be a good source of peptides, amino acids, and minerals for use as organic fertilizer. Traditional feather degradation methods consume large amount of energy and reduces the overall quality of the proteins. However, degradation of keratin by keratinolytic bacteria may represent as an alternative for the development of cheap, cost effective, eco‐friendly, and easily available nitrogen (N) and minerals rich source as potential organic fertilizers. Keratinase enzymes from bacteria are serine‐type proteases showing optimal activity at pH 6 to 9 and 30 to 50 °C. Mechanism of degradation includes, sulfitolysis, proteolysis, followed by deamination. Keratinolytic bacteria showing antagonism against important plant pathogens may act as biocontrol agent. Feather hydrolyzate can also be employed as nitrogenous fertilizers for plant growth. Tryptophan release from the feather degradation can act as precursor for plant phytohormone, indole‐3‐acetic acid (IAA). Solubilization of inorganic phosphate (P) by keratinolytic bacteria may further elevate the growth of plant. Application of hydrolyzate increases the water holding capacity, N, carbon (C) and mineral content of the soil. It elevates protein, amino acids, and chlorophyll content of plant. Feather hydrolyzate enhances seed germination and growth of plant. Soil application further increases the population of beneficial bacteria. The use of keratinolytic bacteria having antagonistic and plant growth promoting activities, and feather hydrolyzate can emerge as sustainable and alternative tools to promote and improve organic farming, agro‐ecosystem, environment, human health, and soil biological activities.

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Section: Discussionmentioning

confidence: 99%

“…Keratins are predominantly composed of cystine, glutamine, lysine, proline, serine, threonine, and valine. However, presence of arginine, histidine, tryptophan, glutamic acid, glycine, isoleucine, leucine, methionine, and phenylalanine are negligible [9][10][11][12][13].…”

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confidence: 99%

Feather degradation by keratinolytic bacteria and biofertilizing potential for sustainable agricultural production

et al. 2018

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“…The presence of sulfur-containing amino acid cysteine in SHG10 FH could support sulphito-lysis mechanism. According to this mechanism, keratinolytic microorganisms cleave disulfide bond included in cysteine of keratin polypeptide chains [17,57]. However, the claimed proposed sulphito-lysis mechanism for feather biodegradation via B. licheniformis SHG10 needs further evidences and experimental investigations in prospective studies.…”

Section: Discussionmentioning

confidence: 99%

A Statistical-Mathematical Model to Optimize Chicken Feather Waste Bioconversion via Bacillus licheniformis SHG10: A Low Cost Effective and Ecologically Safe Approach

S¹

2015

J Bioprocess Biotech

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Feather waste is highly accumulated recalcitrant and non-efficiently utilized protein wastage of poultry processing. Present study highlights a cheap eco-friendly approach towards its valorization into efficiently utilized form (feather hydrolysate (SHG10 FH)) through Bacillus licheniformis SHG10 within 48 hrs. A statistical-mathematical model (Plackett-Burman Design (PBD), Central Composite Design (CCD), Canonical Analysis (CA) and Steepest Rising Ridge (SRR)) was anticipated to optimize feather bioconversion. PBD addressed three key determinants out of eight tested factors imposing significant influence (P≤0.006) on soluble proteins productivity. Optimal levels of the key determinants, localized by CCD, CA and SRR, were 1.55% (w/v) feather, 0.45% (w/v) yeast extract and 10.8% (v/v) inoculum size in basal medium II to attain 402 mg/Liter soluble proteins and 104,000 µmole leucine/Liter NH 2-free amino groups. SHG10 FH was rich in phenylalanine, tyrosine, methionine and histidine. MALDI-TOF-MS showed proteins spectrum of SHG10 FH ranged from 140 Da m/z. to 733 Da m/z. The composition of SHG10 FH along with the ecologically safe low cost effective approach involved in its preparation might underpin its great potential in several industries (e.g., amino acids, soluble proteins, cosmetics and animal feed livestock).

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“…A scan electron microscopy of the biodegraded feather was conducted in line with the described procedures of Gupta and Singh [43]. Briefly, degraded feather at different interval of fermentation was recovered, washed with distilled water and oven-dried at 60 • C, for 24 h. The residual feather was fixed on carbon-sided-tape mounted on the stub and coated with gold palladium for 5 min, using an ion coater (Eiko Engineering Co. Ltd, Hitachinaka, Ibaraki, Japan), and observed under scanning electron microscope (JEOL Ltd, Tokyo Japan).…”

Section: Structural Studies: Scanning Electron Microscopymentioning

confidence: 99%

Bacillus sp. FPF-1 Produced Keratinase with High Potential for Chicken Feather Degradation

2020

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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.

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Hydrolyzing Proficiency of Keratinases in Feather Degradation

Cited by 42 publications

References 20 publications

Feather degradation by keratinolytic bacteria and biofertilizing potential for sustainable agricultural production

Feather degradation by keratinolytic bacteria and biofertilizing potential for sustainable agricultural production

A Statistical-Mathematical Model to Optimize Chicken Feather Waste Bioconversion via Bacillus licheniformis SHG10: A Low Cost Effective and Ecologically Safe Approach

Bacillus sp. FPF-1 Produced Keratinase with High Potential for Chicken Feather Degradation

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