Chicken Feather Meal Research Articles

Nitric Oxide Synthesis Inhibition and Anti-Inflammatory Effect of Polypeptide Isolated from Chicken Feather Meal in Lipopolysaccharide-Stimulated RAW 264.7 Macrophages.

SUMMARYNitric oxide (NO) plays a key role in the pathogenesis of inflammation and has been implicated in endotoxin-induced tissue injury. Chicken feather meal is a rich source of amino acids that may serve as a peptide hydrolysate to inhibit NO activity. Anti-inflammatory hydrolysates of chicken feather meal were prepared and fractionated into five samples based on molecular mass. The smallest fraction (<0.65 kDa) exhibited the highest NO inhibitory activity without cytotoxicity towards macrophage RAW 264.7 cells. Further subfractions were sufficient to obtain amino acid sequences by Q-TOF LC-MS/MS ESI analysis. Of these, the SNPSVAGVR (885.97 Da) peptide and its corresponding pure synthetic peptide have inhibitory activity against NO production by RAW 264.7 cells (IC50=(55.2±0.2) mM) without cytotoxicity. Reverse transcriptase polymerase chain reaction (RT-PCR) and quantitative real-time RT-PCR results revealed that the peptide of the obtained fraction reduced transcript expression levels of the pro-inflammatory cytokines iNOS, TNF-α, COX-2 and IL-6 in lipopolysaccharide-stimulated RAW 264.7 cells. These results suggest that the peptides derived from the chicken feather meal protein could potentially be used as a promising ingredient in functional foods or nutraceuticals against inflammatory diseases.

Substitution of Fish Meal with Chicken Feather Silage Meal on Feed Can Improve Growth Performance of Striped Catfish (Pangasius hypopthalmus)

The purpose of this research is to study the effect of substitution of fish meal with silage meal of chicken feathers on feed to protein digestibility, growth and survival rate of striped catfish (Pangasius hypopthalmus). The test fish used is catfish with an average weight of 2.31 ± 0.04 grams /fish. This research used experimental method with Completely Randomized Design, 5 treatments in triplicate. The treatments in this study were substitution of fish meal meal with different dose of chicken feather meal, namely A, B, C, D and E (0%; 25%; 50%; 75% and 100% silage meal of chicken feathers, respectively). Parameters observed included relative growth rate (RGR), feed conversion ratio (FCR), protein efficiency ratio (PER), Apparent Digestibility Coefficient of Protein (ADCP), and survival rate (SR) of catfish. The results showed that the substitution of fish meal with chicken feather silage meal was very significant (P &lt;0.01) to RGR, FCR, PER, and ADCP, but no significant effect (P&gt; 0.05) on SR of catfish. Dose 25% silage chicken feather meal in the feed is the best dose to improve the RGR and ADCP of catfish. Water quality during the study is still within a reasonable range for catfish culture.

The negative effect of the chicken feather meal in the diet on growth performance of the shortfin eel Anguilla bicolor larvae

The aim of these study was to examine the effect of the replacement fish meal with chicken feather meal (CFM) for eel Anguilla bicolor larvae. The study was conducted at the Laboratory of Ichthyology, Faculty of Marine and Fisheries of Syiah Kuala University on September to October 2017. The Complete Randomized Design (CRD) with 7 treatments and 4 replications were used in this study. The tested dosage of CFM were of 0% CFM (control), 10% CFM, 20% CFM, 30% CFM, 40% CFM, 50% CFM and 60% CFM, where each treatment were contained of protein 32.26% (0% CFM), 33.09% (10% CFM), 36.20% (20% CFM), 39.10% (30% CFM), 41.22% (40% CFM), 45.43 ( 50% CFM) and 40.02% (60% CFM). The experimental fish were stocked in the plastic container at the stocking density of 15 fish container-1 and fed the experimental diets at the feeding level of 10% body weight a day for 60 days. The results showed that the application of CFM in the diet was not given a significant effect on the weight gain, daily weight gain, specific growth rate (P&gt;0.05). In addition, the fish fed on CFM did not show growth rate even reduces the body weight of the experimental fish. It is concluded that the application of the CFM in diet gave the negative effect on the growth performance of the eel larvae.

Using response surface methodology to improve the L-asparaginase production by Aspergillus niger under solid-state fermentation

Abstract Microbial L-asparaginase have been used as a therapeutic agent in the treatment of acute lymphoblastic leukemia and Hodgkin's disease. In addition to clinical use, L-asparaginases have been used in foods to reduce the formation of acrylamide. L- asparaginase production is carried out mainly by submerged fermentation (SmF). However, solid-state fermentation (SSF) offers potential benefits compared with submerged fermentation, such as the use of low-cost agro-industrial residues as the substrate, which is very attractive for bioprocessing. The main objective of this study was to evaluate the use of agro-industrial wastes, including wheat bran, soybean meal, rice meal, chicken feather meal, chicken viscera meal and passion fruit peel flour, for L-asparaginase production by Aspergillus niger LBA 02 under solid-state fermentation. Among the substrates, the highest L-asparaginase activity was obtained using passion fruit peel flour (2380.11 U/gds) after 48 h of fermentation at 30 °C. The effects of temperature, initial moisture content (%) and inoculum concentration (spores/g) on the L-asparaginase production were evaluated using passion fruit peel meal as a substrate using Central Composite Rotatable Design (CCRD) with 17 runs. An increase in L-asparaginase activity (3746.78 U/gds) was obtained using the optimized conditions of passion fruit peel flour with an initial moisture content of 60% and inoculum concentration of 2.1 106 spores/g after 24 h of fermentation at 25 °C. It was observed that the process optimization resulted in a 57% increase in enzyme production compared with the initial values obtained in the “one-factor-at-a-time” method.

Response surface methodology based optimization of keratinase production from Trichoderma harzianum isolate HZN12 using chicken feather waste and its application in dehairing of hide

Keratin proteins are a major constituent of feathers which largely contribute to environmental pollution. The present study reports a potent feather degrading fungi isolated from soil and molecularly characterized (18S rDNA gene sequencing) and identified as Trichoderma harzianum isolate HZN12 (KP235366). Assessment of keratinase production from the isolate revealed better production under solid state fermentation (SSF) conditions (1320 U/g) over submerged (185 U) using chicken feathers. The effect and contribution of independent process variables were studied by Plackett–Burman design. Additionally, statistical modeling by central composite design of response surface methodology was applied to optimize the culture conditions for keratinase production under SSF. Maximum keratinase production (10,150 U/g) was validated with a 7.7 fold increase under the optimized conditions (chicken feather meal 3 g/20 ml, yeast extract 0.2%, glucose 0.9%, pH 8.5 and temperature of 37 °C) with a correlation coefficient (R2) = 95.56%. Keratinase was employed for dehairing of goat hide and assessed based on different organoleptic properties. The keratinase dehaired skin exhibited superior properties in comparison to the chemical treatment. Furthermore, keratinase also showed good stability and compatibility with the tested commercial detergents making it suitable for industrial applications such as, leather and detergent industries. The results suggest an ecofriendly approach for biodegradation of chicken feather waste.

One-Step Ultrafiltration Process for Separation and Purification of a Keratinolytic Protease Produced with Feather Meal

A purification technique to obtain keratinolytic proteases produced byBacillussp. P45 in a medium containing chicken feather meal as substrate is presented. The experiments were carried out in a dead-end ultrafiltration unit, and the influence of the membrane cutoff, pH of enzymatic extract, and operating pressure on the purification of keratinase were studied. The one-step ultrafiltration process with the membrane molecular mass cutoff of 10 kDa at pH 8.0 and operating pressure of 0.147 MPa showed an enzyme recovery of 87.8% and a 4.1-fold purification factor. It is showed that ultrafiltration could be potentially used in the purification of keratinases.

Development and quantification of biodiesel production from chicken feather meal as a cost-effective feedstock by using green technology

Increased urbanization and increase in population has led to an increased demand for fuels. The result is the prices of fuels are reaching new heights every day. Using low-cost feedstocks such as rendered animal fats in biodiesel production will reduce biodiesel expenditures. One of the low-cost feedstocks for biodiesel production from poultry feathers. This paper describes a new and environmentally friendly process for developing biodiesel production technology from feather waste produced in poultry industry. Transesterification is one of the well-known processes by which fats and oils are converted into biodiesel. The reaction often makes use of acid/base catalyst. If the material possesses high free fatty acid then acid catalyst gives better results. The data resulted from gas chromatography (GC) revealed these percentages for fatty acid compositions: myristic acid, palmitic acid, stearic acid, oleic acid, linoleic acid and arachidonic acid. The biodiesel function group was analyzed by using FTIR. This study concluded that the rooster feathers have superior potential to process them into biodiesel than broiler chicken feathers fat because of fatty acid composition values and it has important properties of biodiesel.

PENGGUNAAN PROTEASE DALAM PAKAN YANG MENGGUNAKAN LIMBAH PERTANIAN-PETERNAKAN UNTUK MENINGKATKAN KINERJA PERTUMBUHAN AYAM BROILER

This study was aimed to determine the effects of protease supplementation in diets with agricultural-livestock by products on the growth performance in broiler chickens. The commercial protease used in current study was produced by Bacillus licheniformis which based on keratinase. The treatment diets were a control basal diet without agricultural-livestock by-products and protease supplementation (P1); P1 + 0.05% protease; basal diet with meat bone meal (MBM) and distiller’s dried grain with soluble (DDGS) suppementation (P3); P3 + 0.05% protease (P4); basal diet with hydrolized chicken feather meal (HCFM) and DDGS supplementation (P5); P5 + 0.05% protease. The obtained data were statistically analyzed using Complete Randomized Design, and analyzed subsequently by Orthogonal Contrats Test. Results showed that protease supplementation in the diets containing agricultural-livestock by-products did not affect growth performance of broiler chickens in starter phase and overall age phase. However, in diets containing MBM, protease supplementation reduced the nett gain and feed conversion ratio (FCR) in finisher phase (P&lt;0.05). In diets containing HCFM, protease supplementation increased nett gain and FCR (P&lt;0.05), compared to those of containing MBM. It could be concluded that qualified HCFM, MBM, and DDGS can be used as alternatives for protein-energy source feed stuffs in starter phase, as they did not reduce growth performance of broiler chickens. Protease used in this study might be more effective in diets containing HCFM than those of containing MBM and DDGS.Keywords: Agricultural-livestock by-products, Broilers chickens, Growth performance, Protease.

Effects of protein hydrolysate from chicken feather meal on tyrosinase activity and melanin formation in B16F10 murine melanoma cells.

Tyrosinase is a copper-containing enzyme that controls mammalian melanogenesis. Tyrosinase inhibitors are important for their potential application in cosmetic products. Chicken feather meal is a rich source of amino acids, which have been linked with tyrosinase inhibition activity. This study investigated the tyrosinase inhibitory properties of protein hydrolysates prepared from chicken feather meal. Protein hydrolysates prepared by pepsin-pancreatin with MW <3kDa exhibited strong tyrosinase inhibition activity for both monophenolase (IC50 5.780±0.188µg/mL) and diphenolase activities (IC50 0.040±0.024µg/mL) in a cell-free mushroom tyrosinase system. These samples were uncompetitive inhibitors with Ki values of 18.149 and 27.189µg/mL in monophenolase and diphenolase activities, respectively. A cell culture model showed that this hydrolysate had the strongest inhibition on the viability of B16F10 cells (IC50 1.124±0.288µg/mL) and 0.210µg/mL of the sample exhibited inhibition of tyrosinase activity by 50.493% and melanin synthesis by 14.680% compared to the control.

Alternative fish feed production from waste chicken feathers

&lt;p class="Abstract"&gt;In this This devotion has been done to provide education and training of the utilization of waste chicken manure, making flour chicken feathers as a fish feed alternative, that can overcome some of the problems that waste chicken feathers from the center cutting broiler chickens in the village Krasak enough, it causes pollution, and not used optimally; Low public awareness of awareness of environmental pollution; the lack of public knowledge about the utilization of waste chicken feathers, and processing technology, as well as to address the needs of fish feed more expensive, need alternative feed ingredients. This service program has provided insight to the public about waste chicken feathers so that it can be used as a new entrepreneurial startups. To achieve these objectives have been done of activity as follows: 1) Provide counseling and understanding of the community will be a negative impact on the environment of waste chicken feathers. 2) Provide counseling utilization of waste chicken feathers for people in nearby farms. 3) Make a chicken feather meal of chicken feather waste as an alternative fish feed to improve digestibility of chicken feathers. 3) The formation of the group for increasing the economic income of the family. This service activities program runs quite well with demonstrated some activity, namely: 1) Change Behavior Society (knowledge transfer); 2) Chicken Feather Extension Waste Utilization; 3) Making Unit Waste Chicken Feathers; 4) Establishment of New Business of Diversified Waste Chicken Feathers.&lt;/p&gt;

Effect of Chicken Feather Meal on the Feed Conversion Ratio and Blood Lipid Profile of Broiler Chickens

Effect of Chicken Feather Meal on the Feed Conversion Ratio and Blood Lipid Profile of Broiler Chickens

Purification and partial characterization of serine-metallokeratinase from a newly isolated Bacillus pumilus NRC21

A serine metallokeratinase enzyme (30kDa) produced by a newly isolated Bacillus strain (Bacillus pumilus NRC21) cultivated under optimized conditions in medium containing chicken feather meal was purified and characterized in a set of biochemical assays. The purification was carried out using two successive chromatographic steps; cation exchange chromatography on CM-cellulose and gel filtration on sephadex G-100 columns. The purified enzyme showed a specific activity of 2000units/mg protein against 170units/mg protein for crude extract with 12 fold purification. The enzymatic activity of the keratinase stimulated by (Na+, K+, Mg2+), Hg+2 had no effect, and inhibited by entire tested cations, serine and metalloproteinase inhibitors, therefore it can be considered as a serine metalloenzyme. The optimum pH and temperature for the purified enzyme were (7.5, 8.5) and (50, 45°C) when using keratin azure and azocasein as substrates, respectively. The purified enzyme was highly stable at broad pH and temperature ranged (5–10) and (20–60°C), respectively and its thermoactivity and thermostability were enhanced in the presence of 5mMMg+2. These results suggest that the purified keratinase may be used in several industrial applications.

Supercritical carbon dioxide-based integrated continuous extraction of oil from chicken feather meal, and its conversion to biodiesel in a packed-bed enzymatic reactor, at pilot scale

The continuous production of biodiesel (fatty acid methyl esters; FAME) from chicken feather meal (CFM) was carried out in supercritical carbon dioxide (sc-CO2), in a process combining extraction of oil from CFM followed by transesterification of the CFM oil with methanol. First, extraction experiments were carried out at different pressure, temperature and solvent flow rate conditions to assess the influence of these process parameters on the extraction rate and composition of extracted oil. Over 90% of the oil available in CFM was extracted by sc-CO2 in 60min. Oleic acid (C18:1), palmitic acid (C16:0) and linoleic acid (C18:2) were the major components of the oil extracted, accounting for ca. 84% w/w. The integrated extraction and enzymatic transesterification of CFM oil was then carried out at 40°C and 250bar, at solvent flow rates in the range 30–150g/min, for oil:methanol molar ratios of 1:6–1:24, using Lipozyme RM IM® as biocatalyst, in a pilot plant unit. The lowest FAME yield obtained was 96.7%. Both the extraction and reaction steps were modeled, based on a broken and intact cells approach and the consideration of three consecutive steps, respectively, and a good agreement with experimental data was obtained.

Substitusi Konsentrat Protein Menggunakan Tepung Bulu Ayam yang Diolah Secara Fisiko-Kimia dan Fermentasi Menggunakan Bacillus sp. Mts

(Protein concentrate substitution using feather meal processed by physico-chemistry and fermentatio)ABSTRACT. The objective of this research was to evaluate the effect of protein concentrate substitution using processed feather meal in growing layer-ration. Chicken feather meal was processed by physico-chemical techniques viz.soaking in 0.5% (b/v) NaOH and Na2S at 60°C and continued by fermentation using Bacillus sp. MTS. The method was experimental method with a Completely Randomized Design with five treatments that replicated for four times. The treatments tested was level of concentrate substitution i.e. 0, 4, 8, 12 and 16%. Protein concentrate substitution had no significantly effect (P 0.05) on growth, feed consumption and convertion of growing layer. Keratin meal from chicken feather can be applied in growing layer-ration 16% respectively or substitute the protein concentrate as much as 53%.

Codon Optimization Significantly Improves the Expression Level of a Keratinase Gene in Pichia pastoris

The main keratinase (kerA) gene from the Bacillus licheniformis S90 was optimized by two codon optimization strategies and expressed in Pichia pastoris in order to improve the enzyme production compared to the preparations with the native kerA gene. The results showed that the corresponding mutations (synonymous codons) according to the codon bias in Pichia pastoris were successfully introduced into keratinase gene. The highest keratinase activity produced by P. pastoris pPICZαA-kerAwt, pPICZαA-kerAopti1 and pPICZαA-kerAopti2 was 195 U/ml, 324 U/ml and 293 U/ml respectively. In addition, there was no significant difference in biomass concentration, target gene copy numbers and relative mRNA expression levels of every positive strain. The molecular weight of keratinase secreted by recombinant P. pastori was approx. 39 kDa. It was optimally active at pH 7.5 and 50°C. The recombinant keratinase could efficiently degrade both α-keratin (keratin azure) and β-keratin (chicken feather meal). These properties make the P. pastoris pPICZαA-kerAopti1 a suitable candidate for industrial production of keratinases.

Production and characterization of thermostable metallo-keratinase from newly isolated Bacillus subtilis NRC 3

Novel keratinolytic enzyme (32kDa) secreted by a newly isolated Bacillus strain (Bacillus subtilis NRC3) cultivated in medium containing chicken feather meal was purified and partially characterized in a set of biochemical assays. The purification was carried out by applying a protocol of two successive chromatographic steps; cation exchange chromatography on CM-cellulose and gel filtration on sephadex G-75 columns. The purified enzyme showed a specific activity of 5233units/mg protein against 169units/mg protein for crude extract with 31 fold purification. The enzymatic activity of the purified keratinolytic enzyme stimulated by Na+, K+, Mg2+, Ba2+, Ca2+, and inhibited by entire tested cations and metalloproteinase inhibitors, indicating that it belongs to metallo-keratinase enzymes. The optimum pH and temperature for the purified enzyme were (7.5, 8.0) and (50, 40°C) when using keratin azure and azocasein as substrates, respectively. The purified enzyme was highly stable at broad pH and temperature ranged (5–10) and (20–60°C), respectively. These results suggest that this keratinase may be a useful alternative and ecofriendly route for handling the abundant amount of waste feathers.

우모 케라틴 분해세균의 분리, 특성 및 우모 분해산물의 식물 생육촉진 효과

Abstract This study was conducted to isolate and characterize a novel feather-degrading bacterium producing keratinase activity. A strain K9 was isolated from soil at poultry farm and identified as Xanthomonas sp. K9 by phenotypic characters and 16S rRNA gene analysis. The cultural conditions for the keratinase production were 0.3% fructose, 0.1% gelatin, 0.04% K 2 HPO 4 , 0.06% KH 2 PO 4 , 0.05% NaCl and 0.01% FeSO 4 with an initial pH 8.0 at 30 ℃ and 200 rpm. In an optimized medium containing 0.1% chicken feather, production yield of keratinase was approximately 8-fold higher than the yield in basal medium. The strain K9 effectively degraded chicken feather meal (67%) and duck feather (54%), whereas human nail and human hair showed relatively low degradation rates (13-22%). Total free amino acid concentration in the cell-free supernatant was about 25.799 mg/l. Feather hydrolysate produced by the strain K9 stimulated growth of red pepper, indicating Xanthomonas sp. K9 could be not only used to increase the nutritional value of chicken feather but also a potential candidate for the development of natural fertilizer applicable to crop plant soil. Key Words :Feather, Fertilizer, Keratin, Keratinase

Biosynthesis and Control of Keratinase in Recalcitrant Feather-Degrading Bacillus megaterium F7-1

This study was performed to investigate the nutritional conditions controlling keratinase activity in Bacillus megaterium F7-1. B. megaterium F7-1 produced keratinase using chicken feather as a sole source of carbon, nitrogen and sulfur. Addition of the feather medium with glucose enhanced keratinase production (68.9 U/ml), compared to control without glucose (63.2 U/ml). The synthesis of keratinase was repressed by addition of <TEX>$NH_4Cl$</TEX> in B. megaterium F7-1. The highest keratinase production (70.9 U/ml) was obtained with the feather medium containing glucose and <TEX>$MgSO_4{\cdot}7H_2O$</TEX>. Keratinase was produced in the absence of feather (4.9 U/ml), indicating its constitutive synthesis. Feather degradation resulted in free SH group formation. B. megaterium F7-1 effectively degraded chicken feather meal (86%), whereas duck feather, human nail, human hair and sheep wool displayed relatively low degradation rates (8-34%).

A Novel Serine Metallokeratinase from a Newly Isolated Bacillus pumilus A1 Grown on Chicken Feather Meal: Biochemical and Molecular Characterization

A keratinolytic enzyme (KerA1) secreted by a newly isolated Bacillus pumilus strain A1 cultivated in medium containing chicken feather meal was purified and characterized, and the gene was isolated and sequenced. The molecular mass of the purified enzyme was estimated to be 34,000 Da by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis and gel filtration. The optimum pH and temperature for the purified keratinase were 9.0 and 60 degrees C, respectively, using keratin as a substrate. KerA1 showed a high stability towards nonionic surfactants. It was found to be relatively stable toward the strong anionic surfactant (SDS). The deduced amino acid sequence of the keratinase KerA1 differs from both the organic solvent tolerant protease of B. pumilus 115b and the dehairing protease of B. pumilus UN-31-C-42 by one and nine amino acids, respectively. These results suggest that this keratinase may be a useful alternative and ecofriendly route for handling the abundant amount of waste feathers and for applications in detergent formulations.

Production of Keratinase by Free and Immobilized Cells of Bacillus halodurans Strain PPKS-2: Partial Characterization and Its Application in Feather Degradation and Dehairing of the Goat Skin

An extremely alkaliphilic bacterial strain, Bacillus sp. PPKS-2, was isolated from rice mill effluents and screened for the production of extracellular keratinase. The maximum production of keratinase occurred after 48 h in shaking culture at pH 11.0 and 37 degrees C in a medium containing 0.5% soybean flour. The strain grew and produced alkaline keratinase using chicken feather and horn meal as the sole source of carbon and nitrogen. An addition of 0.1% soybean flour or feather hydrolysate and sodium sulfite to feather medium increased the production and complete solubilization of feather took place within 5 days under solid-state fermentation conditions. The partially purified enzyme displayed maximum activity at pH 11.0 and 60 degrees C in a broad range of NaCl, 0-16%, and was not inhibited by sodium dodecyl sulfate (10%), ethylenediaminetetraacetic acid (10 mM), H2O2 (15%), and other commercial detergents. Immobilization of the whole cells proved to be useful for continuous production of keratinase and feather degradation. The enzyme was effectively used to remove hair from goat hide. The strain PPKS-2 can be effectively used for solid waste management of poultry feather in submerged as well as solid-state fermentation.