An efficient conversion of waste feather keratin into ecofriendly bioplastic film

  • Swati Sharma
  • Arun Gupta
  • Ashok Kumar
  • Chua Gek Kee
  • Hesam Kamyab
  • Syed Mohd Saufi
Original Paper
  • 7 Downloads

Abstract

Feathers biomass from poultry industry is considered as an important waste product, which creates serious environmental problems. In this study, keratin was extracted from waste chicken feathers using sodium sulfide as a reducing agent under optimized conditions. The extracted keratin particles were used to develop a bioploymeric film by adding microcrystalline cellulose as nano-additive agent. The calculated yield of 80.2% was obtained for keratin from feathers dry weight 25 g (w/w). The extracted keratin was characterized using Fourier transform infrared spectroscopy, scanning electron microscopy (SEM), thermogravimetric analysis, differential scanning calorimetry, wide-angle X-ray diffraction. The physiochemical characteristics of the feathers were compared with the keratin powder. The regenerated keratin particles preserved their chemical composition, thermal strength and stability after chemical extraction. The extracted keratin particles showed 10–20-µm spongy porous microparticles in SEM analysis. The keratin powder was used to synthesize a bioplastic film using glycerol (3.5%) and microcrystalline cellulose (0.2%) in NaOH for 48 h at 60 °C. The calculated thickness of bioplastic film was 1.12 × 10−4 mm with tensile strength of 3.62 ± 0.6 MPa. The Young’s modulus and break elongation for synthesized bioplastic film were 1.52 ± 0.34 MPa and 15.8 ± 2.2%, respectively. The feather and keratin showed maximum similarity index of 64.74% (l-alanyl, l-alanyl, l-alanine, p-nitroanilide) and 64.32% with d-pantethine, respectively, using OMNIC Specta software. Overall, the study presented a highly efficient method to convert the waste feather biomass into a bioplastic film which can be used in biopolymer, biomedical and pharmaceutical industries.

Keywords

Poultry waste Feather Keratin Reducing agent Characterization Film synthesis 

Notes

Acknowledgment

Authors are thankful to University Malaysia Pahang (UMP) for proving facilities and financial support; author [SS] is thankful to UMP for providing Doctoral Scholarship Scheme (DSS) scholarship as financial support.

Compliance with ethical standards

Conflict of interest

There is no conflict of interest among all authors.

References

  1. Sharma S et al (2016) Extraction and characterization of keratin from chicken feather waste biomass: a studyGoogle Scholar
  2. Aluigi A, Zoccola M, Vineis C, Tonin C, Ferrero F, Canetti M (2007) Study on the structure and properties of wool keratin regenerated from formic acid. Int J Biol Macromol 41:266–273CrossRefGoogle Scholar
  3. Aluigi A, Vineis C, Varesano A, Mazzuchetti G, Ferrero F, Tonin C (2008) Structure and properties of keratin/PEO blend nanofibres. Eur Polym J 44:2465–2475CrossRefGoogle Scholar
  4. Arai KM, Takahashi R, Yokote Y, Akahane K (1983) Amino-acid sequence of feather keratin from fowl. Eur J Biochem 132:501–507CrossRefGoogle Scholar
  5. Barone JR (2009) Lignocellulosic fiber-reinforced keratin polymer composites. J Polym Environ 17:143–151CrossRefGoogle Scholar
  6. Barone JR, Schmidt WF (2005) Polyethylene reinforced with keratin fibers obtained from chicken feathers. Compos Sci Technol 65:173–181CrossRefGoogle Scholar
  7. Bertsch A, Coello N (2005) A biotechnological process for treatment and recycling poultry feathers as a feed ingredient. Biores Technol 96:1703–1708CrossRefGoogle Scholar
  8. Brandelli A, Sala L, Kalil SJ (2015) Microbial enzymes for bioconversion of poultry waste into added-value products. Food Res Int 73:3–12CrossRefGoogle Scholar
  9. Cao J (2000) Is the α–β transition of keratin a transition of α-helices to β-pleated sheets? Part I. In situ XRD studies. J Mol Struct 553:101–107CrossRefGoogle Scholar
  10. Cavello I, Cavalitto S, Hours R (2012) Biodegradation of a keratin waste and the concomitant production of detergent stable serine proteases from Paecilomyces lilacinus. Appl Biochem Biotechnol 167:945–958CrossRefGoogle Scholar
  11. Dahl KH, McKinley-McKee JS (1981) The reactivity of affinity labels: a kinetic study of the reaction of alkyl halides with thiolate anions—a model reaction for protein alkylation. Bioorg Chem 10:329–341CrossRefGoogle Scholar
  12. Edwards H, Hunt D, Sibley M (1998) FT-Raman spectroscopic study of keratotic materials: horn, hoof and tortoiseshell. Spectrochim Acta Part A Mol Biomol Spectrosc 54:745–757CrossRefGoogle Scholar
  13. Endo R, Kamei K, Iida I, Kawahara Y (2008) Dimensional stability of waterlogged wood treated with hydrolyzed feather keratin. J Archaeol Sci 35:1240–1246CrossRefGoogle Scholar
  14. Eslahi N, Dadashian F, Nejad NH (2013) An investigation on keratin extraction from wool and feather waste by enzymatic hydrolysis. Prep Biochem Biotechnol 43:624–648CrossRefGoogle Scholar
  15. Fang Y, Catron B, Zhang Y, Zhao L, Caruso J, Hu Q (2010) Distribution and in vitro availability of selenium in selenium-containing storage protein from selenium-enriched rice utilizing optimized extraction. J Agric Food Chem 58:9731–9738CrossRefGoogle Scholar
  16. Feughelman M, Lyman D, Willis B (2002) The parallel helices of the intermediate filaments of α-keratin. Int J Biol Macromol 30:95–96CrossRefGoogle Scholar
  17. Fu K, Griebenow K, Hsieh L, Klibanov AM, Langera R (1999) FTIR characterization of the secondary structure of proteins encapsulated within PLGA microspheres. J Controll Release 58:357–366CrossRefGoogle Scholar
  18. Garrido T, Leceta I, de la Caba K, Guerrero P (2018) Chicken feathers as a natural source of sulphur to develop sustainable protein films with enhanced properties. Int J Biol Macromol 106:523–531CrossRefGoogle Scholar
  19. Guo Y, Tang H, Li G, Xie D (2014) Effects of cow dung biochar amendment on adsorption and leaching of nutrient from an acid yellow soil irrigated with biogas slurry. Water Air Soil Pollut 225:1820CrossRefGoogle Scholar
  20. Ha S-W, Tonelli AE, Hudson SM (2005) Structural studies of Bombyx mori silk fibroin during regeneration from solutions and wet fiber spinning. Biomacromolecules 6:1722–1731CrossRefGoogle Scholar
  21. Happey F, Wormell R (1949) 53—Regenerated keratin fibres from wool. J Text Inst Trans 40:T855–T869CrossRefGoogle Scholar
  22. He M, Zhang B, Dou Y, Yin G, Cui Y (2017) Blend modification of feather keratin‐based films using sodium alginate. J Appl Polym Sci 134:44680Google Scholar
  23. Idris A, Vijayaraghavan R, Rana UA, Fredericks D, Patti A, MacFarlane D (2013) Dissolution of feather keratin in ionic liquids. Green Chem 15:525–534CrossRefGoogle Scholar
  24. Idris A, Vijayaraghavan R, Patti A, MacFarlane D (2014) Distillable protic ionic liquids for keratin dissolution and recovery. ACS Sustain Chem Eng 2:1888–1894CrossRefGoogle Scholar
  25. Ji Y, Chen J, Lv J, Li Z, Xing L, Ding S (2014) Extraction of keratin with ionic liquids from poultry feather. Sep Purif Technol 132:577–583CrossRefGoogle Scholar
  26. Jones CB, Mecham D (1943) The dispersion of keratins. I. Studies on the dispersion and degradation of certain keratins by sodium sulfide. Arch Biochem 2:209CrossRefGoogle Scholar
  27. Kamarudin NB, Sharma S, Gupta A, Kee CG, Chik SMSBT, Gupta R (2017) Statistical investigation of extraction parameters of keratin from chicken feather using design-expert. 3 Biotech 7:127CrossRefGoogle Scholar
  28. Khosa MA, Ullah A (2014) In-situ modification, regeneration, and application of keratin biopolymer for arsenic removal. J Hazard Mater 278:360–371CrossRefGoogle Scholar
  29. Lasekan A, Bakar FA, Hashim D (2013) Potential of chicken by-products as sources of useful biological resources. Waste Manag 33:552–565CrossRefGoogle Scholar
  30. Lee H et al (2015) Human hair keratin-based biofilm for potent application to periodontal tissue regeneration. Macromol Res 23:300–308CrossRefGoogle Scholar
  31. Ma B, Qiao X, Hou X, Yang Y (2016) Pure keratin membrane and fibers from chicken feather. Int J Biol Macromol 89:614–621CrossRefGoogle Scholar
  32. Ma B, Chen W, Qiao X, Pan G, Jakpa W, Hou X, Yang Y (2017) Tunable wettability and tensile strength of chitosan membranes using keratin microparticles as reinforcement. J Appl Polym Sci 134:44667Google Scholar
  33. Martelli SM, Moore G, Paes SS, Gandolfo C, Laurindo JB (2006a) Influence of plasticizers on the water sorption isotherms and water vapor permeability of chicken feather keratin films. LWT Food Sci Technol 39:292–301CrossRefGoogle Scholar
  34. Martelli SM, Moore GRP, Laurindo JB (2006b) Mechanical properties, water vapor permeability and water affinity of feather keratin films plasticized with sorbitol. J Polym Environ 14:215–222CrossRefGoogle Scholar
  35. Martinez-Hernandez AL, Velasco-Santos C, De Icaza M, Castano VM (2005) Microstructural characterisation of keratin fibres from chicken feathers. Int J Environ Pollut 23:162–178CrossRefGoogle Scholar
  36. Menefee E, Yee G (1965) Thermally-induced structural changes in wool. Text Res J 35:801–812CrossRefGoogle Scholar
  37. Mohanty AK, Misra M, Drzal LT (2005) Natural fibers, biopolymers, and biocomposites. CRC Press, Boca RatonCrossRefGoogle Scholar
  38. Mokrejs P, Svoboda P, Hrncirik J, Janacova D, Vasek V (2010) Processing poultry feathers into keratin hydrolysate through alkaline-enzymatic hydrolysis. Waste Manag Res 29(3):260–267CrossRefGoogle Scholar
  39. Moore GRP, Martelli SM, Gandolfo C, do Amaral Sobral PJ, Laurindo JB (2006) Influence of the glycerol concentration on some physical properties of feather keratin films. Food Hydrocoll 20:975–982CrossRefGoogle Scholar
  40. Moritz J, Latshaw J (2001) Indicators of nutritional value of hydrolyzed feather meal. Poult Sci 80:79–86CrossRefGoogle Scholar
  41. Nishikawa N, Tanizawa Y, Tanaka S, Horiguchi Y, Asakura T (1998) Structural change of keratin protein in human hair by permanent waving treatment. Polymer 39:3835–3840CrossRefGoogle Scholar
  42. Onifade A, Al-Sane N, Al-Musallam A, Al-Zarban S (1998) A review: potentials for biotechnological applications of keratin-degrading microorganisms and their enzymes for nutritional improvement of feathers and other keratins as livestock feed resources. Biores Technol 66:1–11CrossRefGoogle Scholar
  43. Pavia DL, Lampman GM, Kriz GS, Vyvyan JA (2008) Introduction to spectroscopy. Cengage Learning, BostonGoogle Scholar
  44. Pillai C (2010) Challenges for natural monomers and polymers: novel design strategies and engineering to develop advanced polymers. Des Monomers Polym 13:87–121CrossRefGoogle Scholar
  45. Poole AJ, Church JS (2015) The effects of physical and chemical treatments on Na2S produced feather keratin films. Int J Biol Macromol 73:99–108CrossRefGoogle Scholar
  46. Poole AJ, Church JS, Huson MG (2008) Environmentally sustainable fibers from regenerated protein. Biomacromolecules 10:1–8CrossRefGoogle Scholar
  47. Poole AJ, Lyons RE, Church JS (2011) Dissolving feather keratin using sodium sulfide for bio-polymer applications. J Polym Environ 19:995–1004CrossRefGoogle Scholar
  48. Popescu C, Augustin P (1999) Effect of chlorination treatment on the thermogravimetric behaviour of wool fibres. J Therm Anal Calorim 57:509–515CrossRefGoogle Scholar
  49. Rad ZP, Tavanai H, Moradi A (2012) Production of feather keratin nanopowder through electrospraying. J Aerosol Sci 51:49–56CrossRefGoogle Scholar
  50. Ramakrishnan N, Sharma S, Gupta A, Alashwal BY (2018) Keratin based bioplastic film from chicken feathers and its characterization. Int J Biol Macromol.  https://doi.org/10.1016/j.ijbiomac.2018.01.037 Google Scholar
  51. Rao DR, Gupta V (1992) Crystallite orientation in wool fibers. J Appl Polym Sci 46:1109–1112CrossRefGoogle Scholar
  52. Reddy N, Yang Y (2007) Structure and properties of chicken feather barbs as natural protein fibers. J Polym Environ 15:81–87CrossRefGoogle Scholar
  53. Schrooyen PM, Dijkstra PJ, Oberthür RC, Bantjes A, Feijen J (2000) Partially carboxymethylated feather keratins. 1. Properties in aqueous systems. J Agric Food Chem 48:4326–4334CrossRefGoogle Scholar
  54. Schrooyen PM, Dijkstra PJ, Oberthür RC, Bantjes A, Feijen J (2001a) Partially carboxymethylated feather keratins. 2. Thermal and mechanical properties of films. J Agric Food Chem 49:221–230CrossRefGoogle Scholar
  55. Schrooyen PM, Dijkstra PJ, Oberthür RC, Bantjes A, Feijen J (2001b) Stabilization of solutions of feather keratins by sodium dodecyl sulfate. J Colloid Interface Sci 240:30–39CrossRefGoogle Scholar
  56. Senoz E, Wool RP (2010) Microporous carbon–nitrogen fibers from keratin fibers by pyrolysis. J Appl Polym Sci 118:1752–1765Google Scholar
  57. Sharma S, Gupta A (2016) Sustainable management of keratin waste biomass: applications and future perspectives. Braz Arch Biol Technol 59:e16150684Google Scholar
  58. Sharma S, Gupta A, Chik S, Kee CG, Mistry BM, Kim DH, Sharma G (2017a) Characterization of keratin microparticles from feather biomass with potent antioxidant and anticancer activities. Int J Biol Macromol.  https://doi.org/10.1016/j.ijbiomac.2017.06.015 Google Scholar
  59. Sharma S, Gupta A, Chik SMSBT, Kee CYG, Poddar PK (2017b) Dissolution and characterization of biofunctional keratin particles extracted from chicken feathers. In: IOP conference series: materials science and engineering, vol 1. IOP Publishing, p 012013Google Scholar
  60. Tanabe T, Okitsu N, Tachibana A, Yamauchi K (2002) Preparation and characterization of keratin–chitosan composite film. Biomaterials 23:817–825CrossRefGoogle Scholar
  61. Tesfaye T, Sithole B, Ramjugernath D, Chunilall V (2017) Valorisation of chicken feathers: characterisation of physical properties and morphological structure. J Clean Prod 149:349–365CrossRefGoogle Scholar
  62. Tiwary E, Gupta R (2010) Medium optimization for a novel 58 kDa dimeric keratinase from Bacillus licheniformis ER-15: biochemical characterization and application in feather degradation and dehairing of hides. Biores Technol 101:6103–6110CrossRefGoogle Scholar
  63. Touaibia D, Benayada B (2005) Removal of mercury (II) from aqueous solution by adsorption on keratin powder prepared from Algerian sheep hooves. Desalination 186:75–80CrossRefGoogle Scholar
  64. Ullah A, Vasanthan T, Bressler D, Elias AL, Wu J (2011) Bioplastics from feather quill. Biomacromolecules 12:3826–3832CrossRefGoogle Scholar
  65. Vasconcelos A, Freddi G, Cavaco-Paulo A (2008) Biodegradable materials based on silk fibroin and keratin. Biomacromolecules 9:1299–1305CrossRefGoogle Scholar
  66. Wang Y-X, Cao X-J (2012) Extracting keratin from chicken feathers by using a hydrophobic ionic liquid. Process Biochem 47:896–899CrossRefGoogle Scholar
  67. Wojciechowska E, Włochowicz A, Wesełucha-Birczyńska A (1999) Application of Fourier-transform infrared and Raman spectroscopy to study degradation of the wool fiber keratin. J Mol Struct 511:307–318CrossRefGoogle Scholar
  68. Xu W, Ke G, Wu J, Wang X (2006) Modification of wool fiber using steam explosion. Eur Polym J 42:2168–2173CrossRefGoogle Scholar
  69. Yamauchi K, Yamauchi A, Kusunoki T, Kohda A, Konishi Y (1996) Preparation of stable aqueous solution of keratins, and physiochemical and biodegradational properties of films. J Biomed Mater Res 31:439–444CrossRefGoogle Scholar
  70. Yin X-C, Li F-Y, He Y-F, Wang Y, Wang R-M (2013) Study on effective extraction of chicken feather keratins and their films for controlling drug release. Biomater Sci 1:528–536CrossRefGoogle Scholar
  71. Zhang J et al (2013) Isolation and characterization of biofunctional keratin particles extracted from wool wastes. Powder Technol 246:356–362CrossRefGoogle Scholar
  72. Zhang Y, Zhao W, Yang R (2015) Steam flash explosion assisted dissolution of keratin from feathers. ACS Sustain Chem Eng 3:2036–2042CrossRefGoogle Scholar
  73. Zoccola M, Aluigi A, Tonin C (2009) Characterisation of keratin biomass from butchery and wool industry wastes. J Mol Struct 938:35–40CrossRefGoogle Scholar

Copyright information

© Springer-Verlag GmbH Germany, part of Springer Nature 2018

Authors and Affiliations

  • Swati Sharma
    • 1
  • Arun Gupta
    • 1
  • Ashok Kumar
    • 2
  • Chua Gek Kee
    • 1
  • Hesam Kamyab
    • 3
  • Syed Mohd Saufi
    • 1
  1. 1.Faculty of Chemical Engineering and Natural ResourcesUniversiti Malaysia PahangGambang, KuantanMalaysia
  2. 2.Department of Biotechnology and BioinformaticsJaypee University of Information TechnologyWaknaghat, SolanIndia
  3. 3.Engineering Department, UTM Razak School of Engineering and AdvancedUniversiti Teknologi MalaysiaSkudaiMalaysia

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