Skip to main content
SpringerLink
Log in

Dissolution and regeneration of wool via controlled disintegration and disentanglement of highly crosslinked keratin

  • Published:
Journal of Materials Science Aims and scope Submit manuscript

Abstract

For the first time, pure protein fibers with good mechanical properties were obtained from waste wool after effective de-crosslinking and disentanglement of the highly crosslinked keratin. Every year, more than 1.6 billion pounds of wool keratin-based materials were discarded. Effort has been devoted to convert the keratin resources into high value-added products, especially fibers. In 1940s, pure keratin fibers had been developed from feathers. However, after trying the method, we found the results were not repeatable and did not find any other successful repetition. So far, no effective dissolution and spinning methods have been developed to obtain pure keratin fibers with potential for real applications. In this research, keratin with preserved backbones after de-crosslinking was obtained. Subsequently, surfactant endowed the keratin with satisfactory stretchability for fiber spinning. Fibers of 20 μm with good tensile strength were successfully developed. The technology could be applied onto other highly crosslinked proteins, including feather keratin from poultry industry, sorghum protein and soy protein in bioenergy co-products for production of various industrial products.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6
Fig. 7
Fig. 8
Fig. 9
Fig. 10

Similar content being viewed by others

References

  1. Shishoo R (2012) Technological advances and future challenges. The global textile and clothing industry. Elsevier, Amsterdam, pp 8–28

    Chapter  Google Scholar 

  2. Rauschendorfer LM (2013), Global Development of Fiber Production. http://www.chemistryviews.org/details/news/4723361/Global_Development_of_Fiber_Production.html. Accessed 16 June, 2013

  3. Johnson J, MacDonald S, Meyer L, Norrington B and Skelly C (2014), The World and United States Cotton Outlook,http://www.usda.gov/oce/forum/2014_Speeches/Cotton.pdf. Accessed 2 May, 2014

  4. Chen HL, Burns LD (2006) Environmental analysis of textile products. Cloth Textiles Res J 24:248–261

    Article  Google Scholar 

  5. U.S. Environmental Protection Agency (2013). http://www.epa.gov/osw/conserve/materials/textiles.htm. Accessed 26 Feburary, 2014

  6. Food and Agricultural Organizations of the United Nations (2013). http://faostat.fao.org/site/569/DesktopDefault.aspx?PageID=569#ancor. Accessed 26 Feburary, 2014

  7. Poole AJ, Church JS, Huson MG (2008) Environmentally Sustainable Fibers from Regenerated Protein. Biomacromolecules 10:1–8

    Article  Google Scholar 

  8. Wen G, Naik R, Cookson P, Smith S, Liu X, Wang X (2010) Wool powders used as sorbents to remove Co2+ ions from aqueous solution. Powder Technol 197:235–240

    Article  Google Scholar 

  9. Rajkhowa R, Zhou Q, Tsuzuki T, Morton DA, Wang X (2012) Ultrafine wool powders and their bulk properties. Powder Technol 224:183–188

    Article  Google Scholar 

  10. Yang Y, Reddy N (2013) Potential of using plant proteins and chicken feathers for cotton warp sizing. Cellulose 20(4):2163–2174

    Article  Google Scholar 

  11. Huda S, Yang Y (2009) Feather Fiber Reinforced Light-Weight Composites with Good Acoustic Properties. J Polym Environ 17:131–142

    Article  Google Scholar 

  12. Hu C, Reddy N, Yan K, Yang Y (2011) Acetylation of chicken feathers for thermoplastic applications. J Agri Food Chem 59:10517–10523

    Article  Google Scholar 

  13. Sun P, Liu ZT, Liu ZW (2009) Chemically Modified Chicken Feather as Sorbent for Removing Toxic Chromium (VI) Ions. Ind Eng Chem Res 48:6882–6889

    Article  Google Scholar 

  14. Yang Y, Reddy N (2013) Potential of using plant proteins and chicken feathers for cotton warp sizing. Cellulose 20:2163–2174

    Article  Google Scholar 

  15. Harris M, Brown AE (1947) Natural and Synthetic Protein Fibers. Text Res J 17:323–330

    Article  Google Scholar 

  16. Evans RL, Shore B (1948) U.S. Patent. 2 434 688, Regenerated Keratin

  17. Wormell RL, Happey F (1949) Regenerated Keratin Fibres. Nature 163:18

    Article  Google Scholar 

  18. USDA “Value Added Products from Feather Fiber” $175 K (2004–2006), http://www.eng.auburn.edu/users/royalb/EXPERIENCE.htm (Accessed March 5, 2014)

  19. USDA awards grant $500,000 to develop bio-based products http://www.udel.edu/PR/UDaily/2005/mar/rwool080405.html (Accessed March 5, 2014)

  20. Idris A, Vijayaraghavan R, Rana UA, Fredericks D, Patti AF, MacFarlane DR (2013) Dissolution of feather keratin in ionic liquids. Green Chem 15:525–534

    Article  Google Scholar 

  21. Fan X (2008) Value-added products from chicken feather fibers and protein. Doctoral Thesis. PhD Dissertation, Auburn University, Auburn

  22. Tonin C, Aluigi A, Vineis C, Varesano A, Montarsolo A, Ferrero F (2007) Thermal and structural characterization of poly (ethylene-oxide)/keratin blend films. J Therm Anal Calorim 89:601–608

    Article  Google Scholar 

  23. Aluigi A, Vineis C, Ceria A, Tonin C (2008) Composite biomaterials from fibre wastes: Characterization of wool–cellulose acetate blends. Composites Part A Appl S 39:126–132

    Article  Google Scholar 

  24. Hameed N, Guo Q (2010) Blend films of natural wool and cellulose prepared from an ionic liquid. Cellulose 17:803–813

    Article  Google Scholar 

  25. Iridag Y, Kazanci M (2006) Preparation and characterization of Bombyx mori silk fibroin and wool keratin. J Appl Polym Sci 100:4260–4264

    Article  Google Scholar 

  26. Vasconcelos A, Freddi G, Cavaco-Paulo A (2008) Biodegradable materials based on silk fibroin and keratin. Biomacromolecules 9:1299–1305

    Article  Google Scholar 

  27. Yuan J, Xing ZC, Park SW, Geng J, Kang IK, Shen J, Meng W, Shim KJ, Han IS, Kim JC (2009) Fabrication of PHBV/keratin composite nanofibrous mats for biomedical applications. Macromol Res 17:850–855

    Article  Google Scholar 

  28. Barone JR, Schmidt WF, Liebner CF (2005) Thermally processed keratin films. J Appl Polym Sci 97:1644–1651

    Article  Google Scholar 

  29. Barone JR, Schmidt WF, Gregoire N (2006) Extrusion of feather keratin. J Appl Polym Sci 100:1432–1442

    Article  Google Scholar 

  30. Desnuelle P (1953) In: Neurath H, Bailey K (eds) The Proteins, vol I, Part A. Academic Press, New York, p 87

    Google Scholar 

  31. Jia QX, Xiong ZJ, Shi CM, Zhang LQ, Wang XN (2012) Preparation and properties of polyamide 6 fibers prepared by the gel spinning method. J Appl Polym Sci 124:5165–5171

    Article  Google Scholar 

  32. Tsen C (1969) Effects of oxidizing and reducing agents on changes of flour proteins during dough mixing. Cereal Chem 46:435–442

    Google Scholar 

  33. Ghosh S, Banerjee A (2001) A Multitechnique Approach in Protein/Surfactant Interaction Study: Physicochemical Aspects of Sodium Dodecyl Sulfate in the Presence of Trypsin in Aqueous Medium. Biomacromolecules 3:9–16

    Article  Google Scholar 

  34. Behrendt J, Arevalo E, Gulyas H, Niederste-Hollenberg J, Niemiec A, Zhou J, Otterpohl R (2002) Production of value added products from separately collected urine. Water Sci Technol 46:341–346

    Google Scholar 

  35. Wada M, Takagi H (2006) Metabolic pathways and biotechnological production of l-cysteine. Appl Microbiol Biotechnol 73:48–54

    Article  Google Scholar 

  36. Gallezot P (2007) Process options for converting renewable feedstocks to bioproducts. Green Chem 9:295–302

    Article  Google Scholar 

  37. Long JJ, Cui CL, Wang L, Xu HM, Yu ZJ, Bi XP (2013) Effect of treatment pressure on wool fiber in supercritical carbon dioxide fluid. J Clean Prod 43:52–58

    Article  Google Scholar 

  38. Elsworth FF, Phillips H (1941) The action of sulphites on the cysteine disulphide linkages in wool: The influence of temperature, time and concentration on the reaction. Biochem J 35:135–143

    Google Scholar 

  39. Xu H, Cai S, Xu L, Yang Y (2014) Water-stable three-dimensional ultrafine fibrous scaffolds from keratin for cartilage tissue engineering. Langmuir 30:8461–8470

    Article  Google Scholar 

  40. Xu H, Yang Y (2014) Controlled De-Cross-Linking and Disentanglement of Feather Keratin for Fiber Preparation via a Novel Process. ACS Sustain Chem Eng 2:1404–1410

    Article  Google Scholar 

  41. Xu H, Cai S, Sellers A, Yang Y (2014) Electrospun ultrafine fibrous wheat glutenin scaffolds with three-dimensionally random organization and water stability for soft tissue engineering. J Biotechnol 184:179–186

    Article  Google Scholar 

  42. Xu H, Cai S, Sellers A, Yang Y (2014) Intrinsically water-stable electrospun three-dimensional ultrafine fibrous soy protein scaffolds for soft tissue engineering using adipose derived mesenchymal stem cells. RSC Adv 4:15451–15457

    Article  Google Scholar 

  43. Reddy N, Li Y, Yang Y (2009) Alkali-catalyzed low temperature wet crosslinking of plant proteins using carboxylic acids. Biotechnol Prog 25:139–146

    Article  Google Scholar 

  44. Tanabe T, Okitsu N, Tachibana A, Yamauchi K (2002) Preparation and characterization of keratin–chitosan composite film. Biomaterials 23:817–825

    Article  Google Scholar 

  45. Tanabe T, Okitsu N, Yamauchi K (2004) Fabrication and characterization of chemically crosslinked keratin films. Mater Sci Eng, C 24:441–446

    Article  Google Scholar 

  46. Katoh K, Shibayama M, Tanabe T, Yamauchi K (2004) Preparation and physicochemical properties of compression-molded keratin films. Biomaterials 25:2265–2272

    Article  Google Scholar 

  47. Vasconcelos A, Freddi G, Cavaco-Paulo A (2008) Biodegradable Materials Based on Silk Fibroin and Keratin. Biomacromolecules 9:1299–1305

    Article  Google Scholar 

  48. Katoh K, Shibayama M, Tanabe T, Yamauchi K (2004) Preparation and properties of keratin–poly(vinyl alcohol) blend fiber. J Appl Polym Sci 91:756–762

    Article  Google Scholar 

  49. Hou X, Xu H, Shi Z, Ge M, Chen L, Cao X, Yang Y (2014) Hydrothermal pretreatment for the preparation of wool powders. J Appl Polym Sci. doi:10.1002/app.40173

    Google Scholar 

  50. Tsukada M, Freddi G, Monti P, Bertoluzza A, Kasai N (1995) Structure and molecular conformation of tussah silk fibroin films: Effect of methanol. J Polym Sci, Part B: Polym Phys 33:1995–2001

    Article  Google Scholar 

  51. Xu W, Cui W, Li W, Guo W (2004) Development and characterizations of super-fine wool powder. Powder Technol 140:136–140

    Article  Google Scholar 

Download references

Acknowledgements

This research was financially supported by the Agricultural Research Division at the University of Nebraska-Lincoln, USDA Hatch Act, Multistate Research Project S-1054 (NEB 37-037) and Nebraska Environmental Trust (13-142). The authors thank the AATCC student research grant for Zhuanzhuan Ma. The authors also thank Dr. Han Chen for his help in SEM.

Author information

Authors and Affiliations

  1. Department of Textiles, Merchandising and Fashion Design, University of Nebraska-Lincoln, 234, HECO Building, Lincoln, NE, 68583-0802, USA

    Helan Xu, Zhuanzhuan Ma & Yiqi Yang

  2. Department of Biological Systems Engineering, University of Nebraska-Lincoln, 234, HECO Building, Lincoln, NE, 68583-0802, USA

    Yiqi Yang

  3. Nebraska Center for Materials and Nanoscience, University of Nebraska-Lincoln, 234, HECO Building, Lincoln, NE, 68583-0802, USA

    Yiqi Yang

Authors
  1. Helan Xu
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Zhuanzhuan Ma
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Yiqi Yang
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Yiqi Yang.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Xu, H., Ma, Z. & Yang, Y. Dissolution and regeneration of wool via controlled disintegration and disentanglement of highly crosslinked keratin. J Mater Sci 49, 7513–7521 (2014). https://doi.org/10.1007/s10853-014-8457-z

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10853-014-8457-z

Keywords

Search

Navigation