METHODS OF KERATIN EXTRACTION FROM WOOL AND HAIR AND PROSPECTS OF THEIR APPLICATION IN BIOMEDICINE AND BIOENGINEERING

V. V. Mykhaliuk, V. V. Havryliak


DOI: http://dx.doi.org/10.30970/sbi.1302.600

Abstract


The present article gives the overview of scientific information on the hair structure, the structural and functional properties of keratins, and methods of their extracting from the natural fibers. The article substantiates an importance of keratin extraction by breaking the disulfide bonds and converting the keratin into a soluble form while maintaining
covalent bonds. Such extraction preserves the native properties of these proteins, that ensures their further use as functional biomaterials. The examples of such properties are: resistance of keratin to the effects of chemical and biological factors (due to high frequency of disulfide bonds that make a large number of chemical modifications of proteins possible) and high biocompatibility and low cytotoxicity of keratin-based preparations (due to a similarity of keratin to the extracellular matrix of biological tissues). The keratin-based materials, obtained by this way and then lyophilized, can form fibrillar structures when a particular solvent is selected. The methods of keratins extraction, as well as the efficiency and electrophoretic profiles of obtained extracts, were also analyzed. The purposeful extraction is carried out by the methods based on oxidation, reduction, and sulfitolysis reactions. The oxidation reactions of keratin are irreversible and cause the oxidation of cysteine residues to cysteic acid with the formation of keratosis. At the same time, keratin is obtained due to a reduction reactions. As a result of the reversible process of sulfitolysis, the S-sulfonate anion is formed. The paper also considers promising applications of extracted keratin in biomedicine and bioengineering. The biomedical technologies are related to the effective treatment of hair pathologies. The second area is the creation of keratin-based biomaterials with a wide range of applications, such as tissue engineering, reparative medicine, textile industry, agriculture, cosmetology, and production of cleaning equipment. The third area of keratins application is the identification of a person. Such application makes an important contribution to the anthropological research and forensic science. High resistance of hair proteins to adverse environmental conditions makes this area very promising.


Keywords


hair, keratins, extraction

References


1. Aboushwareb T., Eberli D., Ward C., Broda C., Holcomb J., Atala A., Van Dyke M. A keratin biomaterial gel hemostat derived from human hair: Evaluation in a rabbit model of lethal liver injury. J. Biomed. Mater. Res. B., 2009; 90: 45-54.
Crossref ● PubMed ● Google Scholar

2. Bertrand L., Doucet J., Simionovici A., Tsoucaris G., Walter P. Lead-revealed lipid organisation in human hair. Biochim Biophys Acta, 2003; 1620: 218-224.
Crossref ● Google Scholar

3. Beyer C. The keratin or horny substance of the hair. DE22643. German Pat.,1907.

4. Bouillon C., Wilkinson J.D. The Science of Hair Care. Florida: CRC Press, Taylor & Francis Group., 2005; 752.
Crossref ● Google Scholar

5. Bragulla H.H., Homberger D.G. Structure and functions of keratin proteins in simple, stratified, keratinized and cornified epithelia. J Anat, 2009; 214(4): 516-59.
Crossref ● PubMed ● PMC ● Google Scholar

6. Brown E.-M., Pandya K., Taylor M.-M., Liu C.-K. Comparison of methods for extraction of keratin from waste wool. Agric. Sci., 2016; 7: 670-679.
Crossref ● Google Scholar

7. Conway J.F., Parry D.A.D. Structural features in the heptad substructures and longer range repeats of two-stranded α-fibrous proteins. Int J Biol Macromol, 1990; 12: 328-334.
Crossref ● Google Scholar

8. Coulombe P.A.,Omary M.B. "Hard" and "soft" principles defining the structure, function and regulation of keratin intermediate filaments. Curr Opin Cell Biol, 2002; 14(1): 110-22.
Crossref ● Google Scholar

9. Deb-Choudhury S., Plowman J.E., Harland D.P. Isolation and Analysis of Keratins and Keratin-Associated Proteins from Hair and Wool. Methods in Enzymology, 2016; 568: 279-301.
Crossref ● PubMed ● Google Scholar

10. Deedrick D.W., Koch S.L. Microscopy of hair part 1: a practical guide and manual for human hair. Forensic Sci. Commun., 2004; 6(1): 1-7.
Coogle Scholar

11. Fan J., Liu J.-F., He J.-H. Hierarchy of Wool Fibers and Fractal Dimensions. International Journal of Nonlinear Sciences and Numerical Simulation, 2008; 9(3): 293-296.
Crossref ● Google Scholar

12. Feairheller S.H., Taylor M.M., Windus W., Filachione E.M., Naghski J. Recovery and Analyses of Hair Proteins from Tannery Unhairing Wastes. Journal of Agricultural and Food Chemistry, 1972; 20: 668-670.
Crossref ● PubMed ● Google Scholar

13. Feughelman M., Johnson D. H. Morphology and properties of hair. Hair and hair care, 1997; 1-32.
Crossref
14. Fraser R., David A. Macrofibril assembly in trichocyte (hard α-) keratins. Journal of Structural Biology, 2003; 142: 319-325.
Crossref ● Google Scholar

15. Hamasaki S., Tachibana A., Tada D., Yamauchi K., Tanabe T. Fabrication of highly porous keratin sponges by freeze-drying in the presence of calcium alginate beads. Mater Sci Eng, 2008; 28: 1250-1254.
Crossref ● Google Scholar

16. Harland D.P., Caldwell J.P., Woods J.L., Walls R.J., Bryson W.G. Arrangement of trichokeratin intermediate filaments and matrix in the cortex of Merino wool. J Struct Biol, 2011; 173(1): 29-37.
Crossref ● PubMed ● Google Scholar

17. Hatakeyama R., Tomita Y., Takigami S. Preparation of Water Soluble Wool Keratin and Its Application for Human Hair. Transactons of the Materials Research Society of Japan, 2009; 34: 399-402.
Crossref ● Google Scholar

18. Havryliak V.V., Mykhaliuk V.V. The factors impacting the efficiency of the extraction of keratin wool fibers. Visnyk of Lviv University. Biological Series, 2016; 73: 47-50. (In Ukrainian)
Google Scholar

19. Heid H.W., Moll I., Franke W.W. Patterns of expression of trichocytic and epithelial cytokeratins in mammalian tissues. II. Concomitant and mutually exclusive synthesis of trichocytic and epithelial cytokeratins in diverse human and bovine tissues (hair follicle, nail bed and matrix, lingual papilla, thymic reticulum). Differentiation, 1988; 37(2): 137-157.
Crossref ● PubMed ● Google Scholar

20. Heid H.W., Moll I., Franke W.W. Patterns of expression of trichocytic and epithelial cytokeratins in mammalian tissues. I. Human and bovine hair follicles. Differentiation, 1988; 37(2): 137-157.
Crossref ● PubMed ● Google Scholar

21. Heid H.W., Werner E., Franke W.W. The complement of native α-keratin polypeptides of hair-forming cells: a subset of eight polypeptides that differ from epithelial cytokeratins. Differentiation, 1986; 32(2): 101-119.
Crossref ● PubMed ● Google Scholar

22. Isarankura Na Ayutthaya S., Tanpichai S., Wootthikanokkhan J. Keratin Extracted from Chicken Feather Waste: Extraction, Preparation, and Structural Characterization of the Keratin and Keratin/Biopolymer Films and Electrospuns. Journal of Polymers, 2015; 23(4).
Crossref ● Google Scholar

23. Jones L.N., Rogers G.E., Rufaut N., Sinclair R.D. Location of keratin-associated proteins in developing fiber cuticle cells using immunoelectron microscopy. Int J Trichology, 2010; 2: 89-95.
Crossref ● PubMed ● PMC ● Google Scholar

24. Jones L.N., Simon M., Watts N.R., Booy F.P., Steven A.C., Parry D.A.D. Intermediate filament structure: hard α-Keratin. Biophysical Chemistry, 1997; 68: 83-93.
Crossref ● Google Scholar

25. Katoh K., Shibayama M., Tanabe T., Yamauchi K. Preparation and properties of keratin-poly(vinyl alcohol) blend fiber. J Appl Polym Sci, 2004; 91: 756-762.
Crossref ● Google Scholar

26. Langbein L., Rogers M. A., Winter H. Praetzel S., Beckhaus U., Rackwitz H.R., Schweizer J. The catalog of human hair keratins: I. Expression of the nine type I members in the hair follicle. J Biol Chem, 1999; 274:19874-19893.
Crossref ● PubMed ● Google Scholar

27. Langbein L., Rogers M.A., Winter H., Praetzel S., Schweizer J. The catalog of human hair keratins: II. Expression of the six type II members in the hair follicle and the combined catalog of human type I and type II keratins. J Biol Chem, 2001; 276(37): 35123-35132.
Crossref ● PubMed ● Google Scholar

28. Langbein L., Yoshida H., Praetzel-Wunder S., Parry D.A., Schweizer J. The keratins of the human beard hair medulla: the riddle in the middle. J Invest Dermatol, 2010; 130: 55-73.
Crossref ● PubMed ● Google Scholar

29. Lee, H., Noh, K., Lee, S.C., Kwon, I.K., Han, D.W., Lee, I.S., Hwang, Y.S. Human hair keratin and its-based biomaterials for biomedical applications. Tissue Engineering and Regene­rative Medicine, 2014; 11: 255-265.
Crossref ● Google Scholar

30. Marmer W.N., Dudley R.L. The oxidative degradation of keratin (wool and bovine hair). Journal of the American Leather Chemists Association, 2006; 101: 408-415.
Google Scholar

31. McKinnon A.J., Harland D.P. The role of liquid-crystalline structures in the morphogenesis of animal fibers. Int J Trichology, 2010; 2: 101-103.
Crossref ● PubMed ● PMC ● Google Scholar

32. Naito S., Arai K. Type and location of SS linkages in human hair and their relation to fiber properties in water. J Appl Polym Sci, 1996; 61: 1918-2113.
Crossref ● Google Scholar

33. Nakamura A., Arimoto M., Takeuchi K., Fujii T. A Rapid Extraction Procedure of Human Hair Proteins and Identification of Phosphorylated Species. Biological and Pharmaceutical Bulletin, 2002; 25: 569-572.
Crossref ● PubMed ● Google Scholar

34. Orfanos C.E., Montagna W., Stuttgen G. Hair Research. Springer, 1981; 712 p.
Crossref ● Google Scholar

35. Parker G.J., Leppert T., Anex D.S., Hilmer J.K., Matsunami N., Baird L., et al. Demonstration of Protein-Based Human Identification Using the Hair Shaft Proteome. PLoS One, 2016; 11(9): e0160653.
Crossref ● PubMed ● PMC ● Google Scholar

36. Plowman J.E., Deb-Choudhury S., Bryson W.G., Clerens S., Dyer J.M. Protein expression in orthocortical and paracortical cells of merino wool fibers. J. Agric. Food Chem., 2009; 57(6): 2174-2180.
Crossref ● PubMed ● Google Scholar

37. Plowman J.E., Paton L.N., Bryson W.G. The differential expression of proteins in the cortical cells of wool and hair fibres. Exp Dermatol, 2007; 16(9): 707-714.
Crossref ● PubMed ● Google Scholar

38. Powell B.C., Rogers G.E. Hair keratin: composition, structure and biogenesis. J. Berei­ter-Hahn. Springer, 1986; 695-721.
Crossref ● Google Scholar

39. Rafik M.E., Doucet J., Briki F. The intermediate filament architecture as determined by X-ray diffraction modelling of hard α-keratins. Biophys J, 2004; 86: 3893-39.
Crossref ● PubMed ● PMC ● Google Scholar

40. Rivett D.E., Ward S.W., Belkin L.M., Ramshaw J.A.M., Wilshire J.F.K. The Lennox Legacy. CSIRO Publishing; Collingwood, VIC, Australia: 1996. Keratin and Wool Research.
Crossref ● Google Scholar

41. Rogers G. Laser capture microscopy in a study of expression of structural proteins in the cuticle cells of human hair. Exp Dermatol, 2009; 18: 541-547.
Crossref ● PubMed ● Google Scholar

42. Sando L., Kim M., Colgrave M.L., Ramshaw J.A.M., Werkmeister J.A., Elvin C.M. Photochemical crosslinking of soluble wool keratins produces a mechanically stable biomaterial that supports cell adhesion and proliferation. J Biomed Mater Res A, 2010; 95(3): 901-911.
Crossref ● PubMed ● Google Scholar

43. Shi B., Lu X., Sun D., Cao M. The Mechanism of Oxidative Unhairing Using Hydrogen Pero­xide. Journal of the American Leather Chemists Association, 2003; 98: 185-192.

44. Sierpinski P., Garrett J., Ma J., Apel P., Klorig D., Smith T., Koman L.A., Atala A., Van Dyke M. The use of keratin biomaterials derived from human hair for the promotion of rapid regeneration of peripheral nerves. Biomaterials, 2008; 29: 118-128.
Crossref ● PubMed ● Google Scholar

45. Swift J.A., Smith J.R. Atomic force microscopy of human hair. Scanning, 2000; 22(5): 310-318.
Crossref ● PubMed ● Google Scholar

46. Tachibana A., Kaneko S., Tanabe T., Yamauchi K. Rapid fabrication of keratin-hydroxyapatite hybrid sponges toward osteoblast cultivation and differentiation. Biomaterials, 2005; 26: 297-302.
Crossref ● PubMed ● Google Scholar

47. Tachibana A., Nishikawa Y., Nishino M., Kaneko S., Tanabe T., Yamauchi K. Modified keratin sponge: Binding of bone morphogenetic protein-2 and osteoblast differentiation. J Biosci Bioeng, 2006; 102: 425-429.
Crossref ● PubMed ● Google Scholar

48. Tanabe T., Okitsu N., Tachibana A., Yamauchi K. Preparation and characterization of keratin-chitosan composite film. Biomaterials, 2002; 23: 817-825.
Crossref ● Google Scholar

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

50. Verma V., Verma P., Ray P., Ray A.R. Preparation of scaffolds from human hair proteins for tissue-engineering applications. Biomed Mater, 2008; 3: 25007.
Crossref ● PubMed ● Google Scholar

51. Wagner R., Kiyohara P. K., Silveira M., Joekes I. Electron microscopic observations of human hair medulla. J Microsc, 2007; 226: 54-63.
Crossref ● PubMed ● Google Scholar

52. Wolfram L.J. Human hair: A unique physicochemical composite. J Am Acad Dermatol, 2003; 48: 106-114.
Crossref ● PubMed ● Google Scholar

53. Wrześniewska-Tosik K., Wawro D., Ratajska M., Stęplewski W. Novel composites with feather keratin. Fibres Text. East. Eur., 2007; 15: 157-162.
Google Scholar

54. Yamauchi K., Yamauchi A., Kusunoki T., Kohda A., Konishi Y. Preparation of stable aqueous solution of keratins, and physiochemical and biodegradational properties of films. J. Biomed. Mater. Res.,1996; 31: 439-444.
Crossref ● Google Scholar

55. Zahn H. Jolles P., Hocker H. Formation and Structure of human hair. Birkhauser Verlag, Basel, Switzerland, 1997. Р. 59-148.
Google Scholar

56. Zoccola M., Aluigi A., Vineis C., Tonin C., Ferrero F., Piacentino M.G. Study on cast membranes and electrospun nanofibers made from keratin/fibroin blends. Biomacromolecules, 2008; 9: 2819-2825.
Crossref ● PubMed ● Google Scholar


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