Two species of genus Monopis (M. pavlovskii, M. congestella) from detritus were found in raptorial bird cage. We used feather-traps that include detritus of raptorial bird, each two traps deployed at Mt.Gyeyang in Incheon and Mt.Cheonchuk in Uljin, respectively. Larvae of tineid feed on keratin sources in the detritus of the raptorial bird cage such as pellets, furs, and feathers. Biological information regarding M. pavlovskii and M. congestella and photographs of their immature stage are provided. It is likely that detritus of raptorial bird cage provide a suitable habitat for keratophagous tineids in nature because of a wide variety of keratin in the raptorial bird cage.

제주도의 후기 플라이스토세 퇴적층에서 깃털 화석을 발견하여 기재하였다. 수심이 얕은 바닷가에서 퇴적된 이 퇴적층에서는 사람 발자국을 포함하여 다양한 새 발자국 화석과 포유류 발자국 화석이 풍부하게 산출되었다. 담회색 이암에 밝은 색의 얇은 막으로 잘 보존된 깃털 화석은 깃 판(vane)이 있는 깃털의 일부분이다. 비록 표본의 크기가 길이 10.3 mm, 폭 9.0 mm로 비교적 작지만, 깃대 양쪽에 두 개의 편평한 깃판(vane), 거의 나란하게 휘어진 깃 가지(barbs)그리고 수많은 전면과 후면의 작은 깃 가지(barbules)들이 잘 보존되어 있다. 이 깃털 화석은 국내에서 최초로 발견되어 기재된 것이며 또한 전 세계의 플라이스토세 퇴적층에서도 처음으로 발견된 것이다.

The objective of this study was to investigate the adsorption potential of chicken feathers for the removal of OrangeⅡ (AO7) from aqueous solutions. Batch experiments were performed as a function of different experimental parameters such as initial pH, reaction time, feather dose, initial OrangeⅡ concentration and temperature. The highest OrangeⅡ uptake was observed at pH 1.0. Most of the OrangeⅡ was adsorbed at 2 h and an adsorption equilibrium was reached at 6 h. As the amount of chicken feather was increased, the removal efficiency of Orange II increased up to 99%, but its uptake decreased. By increasing the initial concentration and temperature, OrangeⅡ uptake was increased. The experimental adsorption isotherm exhibited a better fit with the Langmuir isotherm than with the Freundlich isotherm, and maximum adsorption capacity from the Langmuir constant was determined to be 0.179244 mmol/g at 30℃. The adsorption energy obtained from the Dubinin-Radushkevich model was 7.9 kJ/mol at 20℃ and 30℃ which indicates the predominance of physical adsorption. Thermodynamic parameters such as ΔGo, ΔHo, and ΔSo were -12.28 kJ/mol, 20.64 kJ/mol and 112.32 J/mol K at 30℃, respectively. This indicates that the process of OrangeⅡ adsorption by chicken feathers was spontaneous and endothermic. Our results suggest that as a low-cost biomaterials, chicken feather is an attractive candidate for OrangeⅡ removal from aqueous solutions.

Keratin wastes are generated in excess of million tons per year worldwide and biodegradation of keratin by microorganisms possessing keratinase activity can be used as an alternative tool to prevent environmental pollution. For practical use of keratinase, its physicochemical properties should be investigated in detail. In this study, we investigated characteristics of keratinase produced by Xanthomonas sp. P5 which is isolated from rhizospheric soil of soybean. The level of keratinase produced by the strain P5 increased with time and reached its maximum (10.6 U/ml) at 3 days. The production of soluble protein had the same tendency as the production of keratinase. Optimal temperature and pH of keratinase were 40℃-45℃ and pH 9, respectively. The enzyme showed broad temperature and pH stabilities. Thermostability profile showed that the enzyme retained 94.6%-100% of the original activity after 1 h treatment at 10℃-40℃. After treatment for 1 h at pH 6-10, 89.2%-100% of the activity was remained. At pH 11, 71.6% of the original activity was retained after 1 h treatment. Although the strain P5 did not degrade human hair, it degraded duck feather and chicken feather. These results indicate that keratinase from Xanthomonas sp. P5 could be not only used to upgrade the nutritional value of feather hydrolysate but also useful in situ biodegradation of feather.

We investigated the optimal conditions for keratinase production by feather-degrading Pseudomonas geniculata H10 using one variable at a time (OVT) method. The optimal medium composition and cultural condition for keratinase production were determined to be glucose 0.15% (w/v), beef extract 0.08% (w/v), KH2PO4 0.12% (w/v), K2HPO4 0.02% (w/v), NaCl 0.07% (w/v), MgSO4․7H2O 0.03%, MgCl2․6H2O 0.04% along with initial pH 10 at 200 rpm and 25℃, respectively. The production yield of keratinase was 31.6 U/ml in an optimal condition, showing 4.6-fold higher than that in basal medium. The strain H10 also showed plant growth promoting activities. This strain had ammonification activity and produced indoleacetic acid (IAA), siderophore and a variety of hydrolytic enzymes such as protease, lipase and chitinase. Therefore, this study showed that P. geniculata H10 could be not only used to upgrade the nutritional value of feather wastes but also useful in situ biodegradation of feather wastes. Moreover, it is also a potential candidate for the development of biofertilizing agent applicable to crop plant soil.

As byproducts of chicken slaughtering, chicken feathers are produced and mostly discarded without proper treatment, which results in serious environment pollution. Therefore, the appropriate treatment and utilization of chicken feathers are needed. In particular, chicken feathers can be used as protein sources for the preparation of protein hydrolysates, considering that chicken feathers have a large amount of proteins. In this study, chicken feather protein hydrolysates were prepared and their iron-binding peptides were isolated. Chicken feather protein was extracted from feathers of slaughtered chicken, and its hydrolysates were prepared via hydrolysis with Flavourzyme for 8 h. Then the chicken feather protein hydrolysates were ultra-filtered to obtain small peptide fractions and fractionated using Q-Sepharose and Sephadex G-15 columns to isolate their iron-binding peptides. Two major fractions were produced from each of the Q-Sepharose ion exchange chromatography and the Sephadex G-15 gel filtration hromatography. Among the fractions, the peptide fraction with a high iron-binding activity level, F12, was isolated. These results suggest that chicken feather protein hydrolysates can be used as iron supplements.

We investigated usefulness of chicken feather as bioadsorbent for removal of hexavalent chromium[Cr(Ⅵ)] and oil from aqueous solution. Chicken feather was chemically treated with DTPA, EDTA, NaOH and SDS, respectively. Among them, EDTA was the most effective in adsorbing Cr(Ⅵ). Cr(Ⅵ) uptake by chicken feather was increased with decreasing pH; the highest Cr(Ⅵ) uptake was observed at pH 2.0. By increasing Cr(Ⅵ) concentration, Cr(Ⅵ) uptake was increased, and maximum Cr(Ⅵ) uptake was 0.34 mmol/g. Cr(Ⅵ) adsorption by chicken feather was well described by Freundlich isotherm than Langmuir isotherm and Freundlich constant(1/n) was 0.476. As the concentration of chicken feather was increased, Cr (Ⅵ) removal efficiency was increased but Cr(Ⅵ) uptake was decreased. Most of Cr(Ⅵ) was adsorbed at early reaction stage(1 h) and adsorption equilibrium was established at 5 h. On the other hand, chicken feather adsorbed effectively oils including bunker-A and bunker-C. In conclusion, our results suggest that chicken feather waste could be used to remove heavy metal and oil; it is a potential candidate for biosorption material.

We isolated and characterized novel duck feather-degrading bacteria producing keratinase. Twelve strains were isolated from soil and faces at poultry farm, and decayed feathers. They were identified as Bacillus methylotrophicus, Pseudomonas geniculata, Pseudomonas hibiscicola, Exiquobacterium profundum, Bacillus pumilus, Bacillus amyloliquefaciens, Chryseobacterium indologenes, Bacillus thuringiensis, Thermomonas koreensis, respectively, by phenotypic characters and 16S rRNA gene analysis. Generally, the level of keratinase production was not proportional to feather degradation rate. The highest keratinolytic activity was observed in the culture inoculated with Chryseobacterium indologenes D27. Although all strains did not degrade human hair, strains tested effectively degraded chicken feather(53.8-91.4%), wool(40.4-93.0%) and human nail (51.0-82.9%). These results suggest that strains isolated could be not only used to improve the nutritional value of recalcitrant feather waste but also is a potential candidate for biotechnological processes of keratin hydrolysis.

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% K2HPO4, 0.06% KH2PO4, 0.05% NaCl and 0.01% FeSO4 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.

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 NH4Cl in B. megaterium F7-1. The highest keratinase production (70.9 U/ml) was obtained with the feather medium containing glucose and MgSO4·7H2O. 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%).

The aim of this study was to isolate chicken feather-degrading bacteria with high keratinolytic activity and to investigate cultural conditions affecting keratinolytic enzyme production by a selected isolate. A chicken feather-degrading bacterial strain CH3 was isolated from poultry wastes. Isolate CH3 degraded whole chicken feather completely within 3 days. On the basis of phenotypical and 16S rDNA studies, isolate CH3 was identified as Bacillus thuringiensis CH3. This strain is the first B. thuringiensis described as a feather degrader. The bacterium grew with an optimum at pH 8.0 and 37℃, where maximum keratinolytic activity was also observed. The composition of optimal medium for keratinolytic enzyme production was feather 0.1%, sucrose 0.7%, casein 0.3%, K2HPO4 0.03%, KH2PO4 0.04%, MgCl2 0.01% and NaCl 0.05%, respectively. The keratinolytic enzyme had a pH and temperature optima 9.0 and 45℃, respectively. The keratinolytic activity was inhibited ethylenediaminetetraacetic acid, phenylmethylsulfonyl fluoride, and metal ions like Hg2+, Cu2+ and Zn2+. The enzyme activated by Fe2+, dithiothreitol and 2-mercaptoethanol.

Feathers are produced in huge quantities as a waste product at commercial poultry processing plants. Since feathers are almost pure keratin protein, feather wastes represent an alternative to more expensive dietary ingredients for animal feedstuffs. Generally they become feather meal used as animal feed after undergoing physical and chemical treatments. These processes require significant energy and also cause environmental pollutions. Therefore, biodegradation of feather by microorganisms represents an alternative method to prevent environment contamination. The aim of this study was to investigate cultural conditions affecting keratinolytic protease production by Bacillus pumilus RS7. We also assessed the nutritive value of microbial and alkaline feather hydrolysates. The composition of optimal medium for the keratinolytic protease was fructose 0.05%, yeast extract 0.3%, NaCl 0.05%, K2HPO4 0.03%, KH2PO4 0.04% and MgCl2ㆍ6H2O 0.01%, respectively. The optimal temperature and initial pH was 30℃ and 9.0, respectively. The keratinolytic protease production under optimal condition reached a maximum after 18 h of cultivation. Total amino acid content of feather hydrolysates treated by NaOH and B. pumilius RS7 was 113.8 ㎍/ml and 504.9 ㎍/ml, respectively. Essential amino acid content of feather hydrolysates treated by NaOH and B. pumilius RS7 was 47.2 ㎍/ml and 334.0 ㎍/ml, respectively. Thus, feather hydrolysates have the potential for utilization as an ingredient in animal feed.

The aim of this study was to isolate mesophilic chicken feather-degrading bacteria and to evaluate feather hydrolysate as alternative biofertilizer. Isolate RS7 was isolated from compost and identified as Bacillus pumilus according to API analysis and 16S rDNA sequencing analysis. Chicken feathers were completely degraded after 5 days of cultivation at 30℃. Feather hydrolysate treated by B. pumilius RS7 positively influenced Helianthus sannuus L. (sunflower) growth (e.g. growth rate, number and dry weight of leave, and flowering rate). These results suggest that feather hydrolysate prepared using B. pumilius RS7 could successfully be used as alternative biofertilizer, thereby reducing the environmental impact of feather waste from the poultry industry.