Keratin Production and Its Applications: Current and Future Perspective

  • Anshuman Shah
  • Shaily Tyagi
  • Ram Naresh Bharagava
  • Dalel Belhaj
  • Ashok Kumar
  • Gaurav Saxena
  • Ganesh Dattatraya Saratale
  • Sikandar I. MullaEmail author
Part of the Springer Series on Polymer and Composite Materials book series (SSPCM)


Keratin is a global class of biological material, which represents a group of cysteine-rich filament-forming proteins. They serve as a shielding layer for the epidermal appendages like nails, claws, beak, hair, wool, horns, and feathers. These proteins are further subdivided into two different class based on their secondary structure: α-keratin and β-keratin. Keratin is insoluble in hot or cold water; this unique property helps to prevent their digestion by proteolytic enzymes. Additionally, their complex hierarchical-like filament-matrix structure at nanoscale and the polypeptide chains create a robust wall for protection against heat stress, pathogen invasions (particularly through skin), mechanical damage, etc. In this review, we are trying to attempt a linear focus in the direction of structure, function, extraction of keratin, and its industrial applications.


Keratin Keratin structure Keratin production Keratin application 



The authors are very thankful to the Mr. Chaitanya Sharma and Ms. Arshia Gupta for their valuable suggestions during designing of 3D structure of keratin protein.


  1. Abdel-Naby MA, El-Refai HA, Ibrahim MHA (2017) Structural characterization, catalytic, kinetic and thermodynamic properties of keratinase from Bacillus pumilus FH9. Int J Biol Macromol 105:973–980CrossRefGoogle Scholar
  2. Agrahari S, Wadhwa N (2010) Degradation of chicken feather a poultry waste product by keratinolytic bacteria isolated from dumping site at Ghazipur poultry processing plant. Int J Poult Sci 9:482–489CrossRefGoogle Scholar
  3. Alibardi L, Dalla Valle L, Toffolo V, Toni M (2006) Scale keratin in lizard epidermis reveals amino acid regions homologous with avian and mammalian epidermal proteins. Anat Rec A Discov Mol Cell Evol Biol 288:734–752CrossRefGoogle Scholar
  4. Astbury WT, Marwick TC (1932) X-ray interpretation of the molecular structure of feather keratin. Nature 130:309–310CrossRefGoogle Scholar
  5. Astbury WT, Woods HJ (1934) X-ray studies of the structure of hair, wool, and related fibres. II. The molecular structure and elastic properties of hair keratin. Trans R Soc (London) 232:333–394CrossRefGoogle Scholar
  6. Bagewadi ZK, Mulla SI, Ninnekar HZ (2018) Response surface methodology-based optimization of keratinase production from Trichoderma harzianum isolate HZN12 using chicken feather waste and its application in dehairing of hide. J Environ Chem Eng 6:4828–4839CrossRefGoogle Scholar
  7. Bear RS, Rugo HJ (1951) The results of X-ray diffraction studies on keratin fibers. Ann N Y Acad Sci 53:627–648CrossRefGoogle Scholar
  8. Bohacz J (2017) Biodegradation of feather waste keratin by a keratinolytic soil fungus of the genus Chrysosporium and statistical optimization of feather mass loss. World J Microbiol Biotechnol 33:13CrossRefGoogle Scholar
  9. Chen PY, McKittrick J, Meyers MA (2012) Biological materials: functional adaptations and bioinspired designs. Prog Mater Sci 57:1492–1704CrossRefGoogle Scholar
  10. Chitturi MKCh, Lakshmi VV (2016) Development of semi-solid state fermentation of Keratinase and optimization of process by cheaper and alternative agricultural wastes. Eur J Biotechnol Biosci 4:1–4Google Scholar
  11. Cook J, Gordon JE, Evans CC, Marsh DM (1964) A mechanism for the control of crack propagation in all-brittle systems. Proc R Soc Lond A 282:508–520CrossRefGoogle Scholar
  12. Coulombe PA, Wong P (2004) Cytoplasmic intermediate filaments revealed as dynamic and multipurpose scaffolds. Nat Cell Biol 6:699–706CrossRefGoogle Scholar
  13. Coulombe PA, Lee CH (2012) Defining keratin protein function in skin epithelia: epidermolysis bullosa simplex and its aftermath. J Invest Dermatol 132:763–775CrossRefGoogle Scholar
  14. Crick F (1952) Is [α]-keratin a coiled coil? Nature 170:882–883CrossRefGoogle Scholar
  15. Crick FH (1953) The packing of α-helices: simple coiled-coils. Acta Cryst 6:689–697CrossRefGoogle Scholar
  16. Dalla Valle L, Michieli F, Benato F, Skobo T, Alibardi L (2013) Molecular characterization of alpha-keratins in comparison to associated beta-proteins in soft-shelled and hard-shelled turtles produced during the process of epidermal differentiation. J Exp Zool Part B Mol Dev Evol 320:428–441Google Scholar
  17. Eggum BO (1970) Evaluation of protein quality of feather meal under different treatments. Acta Agricul Scand 20:230–234CrossRefGoogle Scholar
  18. Fellahi S, GAD MH, Zaghlou TI, Feuk-Lagerstedt E, Taherzadeh MJ (2014) A Bacillus strain able to hydrolyze α- and β-keratin. J Bioprocess Biotech 4:181CrossRefGoogle Scholar
  19. Feughelman M (1997) Mechanical properties and structure of alpha-keratin fibers: wool, human hair and related fibers. University of New South Wales PressGoogle Scholar
  20. Filshie BK, Gogers GE (1962) An electron microscope study of the fine structure of feather keratin. J Cell Biol 13:1–12CrossRefGoogle Scholar
  21. Filshie BK, Fraser RD, MacRae TP, Rogers GE (1964) X-ray-diffraction and electron-microscope observations on soluble derivatives of feather keratin. Biochemical J  92(1):18–2Google Scholar
  22. Fraser RD, Parry DA (2008) Molecular packing in the feather keratin filament. J Struct Biol 162:1–13CrossRefGoogle Scholar
  23. Fraser RD, Parry DA (2011) The structural basis of the filament-matrix texture in the avian/reptilian group of hard β-keratins. J Struct Biol 173:391–405CrossRefGoogle Scholar
  24. Fraser RDB, MacRae TP, Rogers GE (1972) Keratins: their composition, structure and biosynthesis. ThomasGoogle Scholar
  25. Fuchs E, Cleveland DW (1998) A structural scaffolding of intermediate filaments in health and disease. Science 279:514–519CrossRefGoogle Scholar
  26. Fujii T, Ogiwara D, Arimoto M (2004) Convenient procedures for human hair protein films and properties of alkaline phosphatase incorporated in the film. Biol Pharm Bull 27:89–93CrossRefGoogle Scholar
  27. Geist V (1966) The evolution of horn-like organs. Behavior 27:175–214CrossRefGoogle Scholar
  28. Gousterova A, Nustorova M, Goshev I, Christov P, Braikova D, Tishinov K, Haertle T, Nedkov P (2003) Alkaline hydrolysate of waste sheep wool aimed as fertilizer. Biotechnol Biotechnol Equip 17:140–145CrossRefGoogle Scholar
  29. Gregg K, Wilton SD, Parry DA, Rogers GE (1984) A comparison of genomic coding sequences for feather and scale keratins: structural and evolutionary implications. EMBO J 3:175–178CrossRefGoogle Scholar
  30. Hammond C, Than M, Walker J (2010) From the laboratory to the leg: patient’s and nurses perceptions of product application using three different dressing formats. Wound Pract Res 18:189–195Google Scholar
  31. Hamrick MW (1998) Functional and adaptive significance of primate pads and claws: evidence from New World anthropoids. Am J Phys Anthropol 106:113–127CrossRefGoogle Scholar
  32. Kadir M, Wang X, Zhu B, Liu J, Harland D, Popescu C (2017) The structure of the “amorphous” matrix of keratins. J Struct Biol 198:116–123CrossRefGoogle Scholar
  33. Karthikeyan R, Balaji S, Sehgal PK (2007) Industrial applications of keratins—a review. J Sci Ind Res 66:710–715Google Scholar
  34. Kim S, Coulombe PA (2007) Intermediate filament scaffolds fulfill mechanical, organizational, and signaling functions in the cytoplasm. Genes Dev 21:1581–1597CrossRefGoogle Scholar
  35. Lee SH, Jun SH, Yeom J, Park SG, Lee CK, Kang NG (2018) Optical clearing agent reduces scattering of light by the stratum corneum and modulates the physical properties of coenocytes via hydration. Skin Res Technol. Scholar
  36. Lewis DM, Rippon JA (2013) The coloration of wool and other keratin fibres. Scholar
  37. Li QM, Zhu LJ, Liu RG, Huang D, Jin X, Che N, Li Z, Qu XZ, Kang HL, Huang Y (2012) Biological stimuli responsive drug carriers based on keratin for triggerable drug delivery. J Mater Chem 22:19964–19973CrossRefGoogle Scholar
  38. Loan F, Cassidy S, Marsh C, Simcock J (2016) Keratin-based products for effective wound care management in superficial and partial thickness burns injuries. Burns 42:541–547CrossRefGoogle Scholar
  39. Luester AU (2006) Manual of Pirrot behavior. Wiley Blackwell PublishingGoogle Scholar
  40. Malafaya PB, Silva GA, Reis RL (2007) Natural-origin polymers as carriers and scaffolds for biomolecules and cell delivery in tissue engineering applications. Adv Drug Deliv Rev 59:207–233CrossRefGoogle Scholar
  41. Mano JF, Silva GA, Azevedo HS, Malafaya PB, Sousa RA, Silva SS, Boesel LF, Oliveira JM, Santos TC, Marques AP, Neves NM, Reis RL (2007) Natural origin biodegradable systems in tissue engineering and regenerative medicine: present status and some moving trends. J R Soc Interface 4:999–1030CrossRefGoogle Scholar
  42. Meyers MA, Chen P-Y, Lin AY-M, Seki Y (2008) Biological materials: structure and mechanical properties. Prog Mater Sci 53:1–206CrossRefGoogle Scholar
  43. Nair L, Laurencin C (2006) Polymers as biomaterials for tissue engineering and controlled drug delivery. Adv Biochem Eng Biotechnol 102:47–90PubMedGoogle Scholar
  44. Nelson JL, Roeder BL, Carmen JC, Roloff F, Pitt WG (2002) Ultrasonically activated chemotherapeutic drug delivery in a rat model. Cancer Res 62:7280–7283PubMedGoogle Scholar
  45. Niculescu M-D, Berechet MD, Gaidau C, Ignat M, Radu M (2016) Study on obtaining keratin extracts from leather industry by-products, ICAMS (2016). In: 6th international conference on advanced materials and systems.
  46. Onifade AA, Al-Sane NA, Al-Musallam AA, 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
  47. Papadopoulos MC, El Boushy AR, Ketelaars EH (1985) Effect of different processing conditions on amino acid digestibility of feather meal determined by chicken assay. Poult Sci 64:1729–1741CrossRefGoogle Scholar
  48. Parveen S, Sahoo SK (2008) Polymeric nanoparticles for cancer therapy. J Drug Target 16:108–123CrossRefGoogle Scholar
  49. Rouse JG, Van Dyke ME (2010) A review of keratin-based biomaterials for biomedical applications. Materials 3:999–1014CrossRefGoogle Scholar
  50. Saratale GD, Kshirsagar SD, Sampange VT, Saratale RG, Oh SE, Govindwar SP, Oh MK (2014) Cellulolytic enzymes production by utilizing agricultural wastes under Solid State Fermentation and its application for Biohydrogen production. Appl Biochem Biotechnol 174:2801–2817CrossRefGoogle Scholar
  51. Schweizer J, Bowden PE, Coulombe PA, Langbein L, Lane EB, Magin TM, Maltais L, Omary MB, Parry DA, Rogers MA, Wright MW (2006) New consensus nomenclature for mammalian keratins. J Cell Biol 174:169–174CrossRefGoogle Scholar
  52. Sharma S, Gupta A (2016) Sustainable management of keratin waste biomass: applications and future perspectives. Braz Arch Biol Technol 59Google Scholar
  53. 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. Scholar
  54. 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
  55. Sharma S, Gupta A, Chik SMST, Kee CYG, Podder PK, Subramaniam M, Thuraisingam J (2017c) Study of different treatment methods on chicken feather biomass. IIUM Eng J 18(2):47–55CrossRefGoogle Scholar
  56. Sharma S, Gupta A, Kumar A, Kee CG, Kamyab H, Saufi SM (2018) An efficient conversion of waste feather keratin into ecofriendly bioplastic film. Clean Technol Environ Policy 1–11Google Scholar
  57. Sharma S, Gupta A, Saufi SM, Chik T, Chua GK, Pradeep Kumar P, Jayshree T, Malini S (2016) Extraction and characterization of keratin from chicken feather waste biomass: a studyGoogle Scholar
  58. Shavandi A, A Bekhit AE-D, Carne A, Bekhit A (2017a) Evaluation of keratin extraction from wool by chemical methods for bio-polymer application. J Bioact Compat Polym 32:163-177Google Scholar
  59. Shavandi A, Silva TH, Bekhit AA, Bekhit AEA (2017b) Keratin: dissolution, extraction and biomedical application. Biomater Sci 5:1699–1735CrossRefGoogle Scholar
  60. Sinkiewicz I, Sliwinska A, Staroszczyk H, Kołodziejska I (2017) Alternative methods of preparation of soluble keratin from chicken feathers. Waste Biomass Valor 8:1043–1048CrossRefGoogle Scholar
  61. Soccol CR, da Costa ESF, Letti LAJ, Karp SG, Woiciechowski AL, de Souza Vandenberghe LP (2017) Recent developments and innovations in solid state fermentation. Biotechnol Res Innov 1:52–71CrossRefGoogle Scholar
  62. Staron P, Banach M, Kowalski Z (2011) Keratin-Origins, properties, application. Chemik 65:1019–1026Google Scholar
  63. Steinert PM, Idler WW, Zimmerman S (1976) Self-assembly of bovine epidermal keratin filaments in vitro. J Mol Biol 108:547–567CrossRefGoogle Scholar
  64. Tang L, Sierra JO, Kelly R, Kirsner RS, Li J (2012) Wool-derived keratin stimulates human keratinocyte migration and types IV and VII collagen expression. Exp Dermatol 21:458–460CrossRefGoogle Scholar
  65. Tesfaye T, Sithole B, Ramjugernath D, Chunilall V (2017) Valorisation of chicken feathers: characterisation of chemical properties. Waste Manag 68:626–635CrossRefGoogle Scholar
  66. Than MP, Smith RA, Cassidy S, Kelly R, Marsh C, Maderal A, Kirsner RS (2013) Use of a keratin-based hydrogel in the management of recessive dystrophic epidermolysis bullosa. J Dermatol Treat 24:290–291CrossRefGoogle Scholar
  67. Tiwary E, Gupta R (2012) Rapid conversion of chicken feather to feather meal using dimeric keratinase from Bacillus licheniformis ER-15. J Bioprocess Biotech 2:123CrossRefGoogle Scholar
  68. Tombolato L, Novitskaya EE, Chen PY, Sheppard FA, McKittrick J (2010) Microstructure, elastic properties and deformation mechanisms of horn keratin. Acta Biomater 6:319–330CrossRefGoogle Scholar
  69. Tomlinson DJ, Mülling CH, Fakler TM (2004) Invited review: formation of keratins in the bovine claw: roles of hormones, minerals, and vitamins in functional claw integrity. J Dairy Sci 87:797–809CrossRefGoogle Scholar
  70. Trim MW, Horstemeyer MF, Rhee H, El Kadiri H, Williams LN, Liao J, Walters KB, McKittrick J, Park SJ (2011) The effects of water and microstructure on the mechanical properties of bighorn sheep (Ovis canadensis) horn keratin. Acta Biomater 7:1228–1240CrossRefGoogle Scholar
  71. U.S Patent No. 7,169,896 (2007) Keratin-based products and methods for their productions. USAGoogle Scholar
  72. Vasconcelos A, Pêgo AP, Henriques L, Lamghari M, Cavaco-Paulo A (2010) Protein matrices for improved wound healing: elastase inhibition by a synthetic peptide model. Biomacromolecules 11:2213–2220CrossRefGoogle Scholar
  73.  Wang J, Hao S, Luo T, Yang Q, Wang B (2016a) Development of feather keratin nanoparticles and investigation of their hemostatic efficacy. ‎Mater Sci Eng C 68:768–773CrossRefGoogle Scholar
  74. Wang B, Yang W, McKittrick J, Meyers MA (2016b) Keratin: structure, mechanical properties, occurrence in biological organisms, and efforts at bioinspiration. Prog Mater Sci 76:229–318CrossRefGoogle Scholar

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© Springer Nature Switzerland AG 2019

Authors and Affiliations

  • Anshuman Shah
    • 1
  • Shaily Tyagi
    • 1
  • Ram Naresh Bharagava
    • 2
  • Dalel Belhaj
    • 3
  • Ashok Kumar
    • 4
  • Gaurav Saxena
    • 2
  • Ganesh Dattatraya Saratale
    • 5
  • Sikandar I. Mulla
    • 6
    • 7
    Email author
  1. 1.ICAR-National Research Centre on Plant BiotechnologyNew DelhiIndia
  2. 2.Laboratory of Bioremediation and Metagenomics Research (LBMR), Department of Environmental Microbiology (DEM)Babasaheb Bhimrao Ambedkar University (A Central University)LucknowIndia
  3. 3.Laboratory of Biodiversity and Aquatic Ecosystems Ecology and Planktonology, Department of Life SciencesUniversity of Sfax-Tunisia, FSSSfaxTunisia
  4. 4.Department of Biotechnology and BioinformaticsJaypee University of Information TechnologyWaknaghat, SolanIndia
  5. 5.Department of Food Science and BiotechnologyDongguk University-SeoulGoyang-SiRepublic of Korea
  6. 6.Key Laboratory of Urban Pollutant Conversion, Institute of Urban EnvironmentChinese Academy of SciencesXiamenChina
  7. 7.Department of BiochemistryKarnatak UniversityDharwadIndia

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