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Journal of Material Cycles and Waste Management

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06-10-2022 | REVIEW

Extraction of keratin from keratinous wastes: current status and future directions

Authors: Neeharika Senthilkumar, Snehaunshu Chowdhury, Pallab Sanpui

Published in: Journal of Material Cycles and Waste Management | Issue 1/2023

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Abstract

This review aims to trace the developments of keratin extraction techniques over the last 70 years and possibilities for future research. Keratin is a fibrous structural protein naturally present in the appendages of animals such as hair, wool, feathers, hooves and hides. Currently millions of tons of these appendages are discarded as waste products by the meat, poultry, textile and leather industries. These keratin-rich wastes lack environmental-friendly disposal methods, and are often dumped in landfills or incinerated. Over the last few years, several studies have developed various methods to repurpose these wastes as a potential source for obtaining keratin. Keratin has recently been demonstrated to have applications within the biomedical field (as a scaffold material in tissue engineering, for drug delivery and wound healing), cosmetic products and environmental remediation. To meet the demand for keratin in the above-mentioned applications, research on extracting keratin from different natural sources including keratinous wastes and improving the extraction efficiency thereof is imperative. Hence, with a brief introduction to the structure and occurrence of keratin, the present review extensively focuses on current methods of its extraction from hair, feathers, wool, hides and hooves. Also, the review identifies gaps in current research and outlines future directions in this field.

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Sharma S, Gupta A, Kumar A (2019) Keratin: an introduction. In: Sharma S, Kumar A (eds) Keratin as a protein biopolymer springer series on polymer and composite materials. Springer, Cham, pp 1–18CrossRef

Feroz S, Muhammad N, Ratnayake J, Dias G (2020) Keratin-based materials for biomedical applications. Bioact Mater 5:496–509. https://doi.org/10.1016/j.bioactmat.2020.04.007CrossRef

McKittrick J, Chen PY, Bodde SG, Yang W, Novitskaya EE, Meyers MA (2012) The structure, functions, and mechanical properties of keratin. Jom 64:449–468. https://doi.org/10.1007/s11837-012-0302-8CrossRef

Wang B, Yang W, McKittrick J, Meyers MA (2016) Keratin: Structure, mechanical properties, occurrence in biological organisms, and efforts at bioinspiration. Prog Mater Sci 76:229–318. https://doi.org/10.1016/j.pmatsci.2015.06.001CrossRef

Peyton CC, Keys T, Tomblyn S, Burmeister D, Beumer JH, Holleran JL et al (2012) Halofuginone infused keratin hydrogel attenuates adhesions in a rodent cecal abrasion model. J Surg Res 178:545–552. https://doi.org/10.1016/j.jss.2012.07.053CrossRef

Kim SY, Park BJ, Lee Y, Park NJ, Park KM, Hwang YS et al (2019) Human hair keratin-based hydrogels as dynamic matrices for facilitating wound healing. J Ind Eng Chem 73:142–151. https://doi.org/10.1016/j.jiec.2019.01.017CrossRef

Barba C, Méndez S, Roddick-Lanzilotta A, Kelly R, Parra JL, Coderch L (2008) Cosmetic effectiveness of topically applied hydrolysed keratin peptides and lipids derived from wool. Skin Res Technol 14:243–248. https://doi.org/10.1111/j.1600-0846.2007.00280.xCrossRef

Shah A, Tyagi S, Bharagava RN, Belhaj D, Kumar A, Saxena G et al (2019) Keratin production and its applications: current and future perspective. In: Sharma S, Kumar A (eds) Keratin as a protein biopolymer. Springer, Cham, pp 19–34CrossRef

O’brien FJ (2011) Biomaterials and scaffolds for tissue engineering. Mater Today 14:88–95. https://doi.org/10.1016/S1369-7021(11)70058-XCrossRef

10.

Balaji S, Kumar R, Sripriya R, Kakkar P, Ramesh DV, Reddy PN et al (2012) Preparation and comparative characterization of keratin-chitosan and keratin-gelatin composite scaffolds for tissue engineering applications. Mater Sci Eng C 32:975–982. https://doi.org/10.1016/j.msec.2012.02.023CrossRef

11.

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. https://doi.org/10.1021/la500768bCrossRef

12.

Yue K, Liu Y, Byambaa B, Singh V, Liu W, Li X et al (2018) Visible light crosslinkable human hair keratin hydrogels. Bioeng Transl Med 3:37–48. https://doi.org/10.1002/btm2.10077CrossRef

13.

Wang S, Wang Z, Foo SE, Tan NS, Yuan Y, Lin W et al (2015) Culturing fibroblasts in 3D human hair keratin hydrogels. ACS Appl Mater Interfaces 7:5187–5198. https://doi.org/10.1021/acsami.5b00854CrossRef

14.

Lin CW, Chen YK, Tang KC, Yang KC, Cheng NC, Yu J (2019) Keratin scaffolds with human adipose stem cells: physical and biological effects toward wound healing. J Tissue Eng Regen Med 13:1044–1058. https://doi.org/10.1002/term.2855CrossRef

15.

Borrelli M, Joepen N, Reichl S, Finis D, Schoppe M, Geerling G et al (2015) Keratin films for ocular surface reconstruction: Evaluation of biocompatibility in an in-vivo model. Biomaterials 42:112–120. https://doi.org/10.1016/j.biomaterials.2014.11.038CrossRef

16.

Tomblyn S, Pettit Kneller EL, Walker SJ, Ellenburg MD, Kowalczewski CJ et al (2016) Keratin hydrogel carrier system for simultaneous delivery of exogenous growth factors and muscle progenitor cells: keratin hydrogels for growth factor and cell delivery. J Biomed Mater Res B Appl Biomater 104:864–879. https://doi.org/10.1002/jbm.b.33438CrossRef

17.

Passipieri JA, Baker HB, Siriwardane M, Ellenburg MD, Vadhavkar M, Saul JM et al (2017) Keratin hydrogel enhances in vivo skeletal muscle function in a rat model of volumetric muscle loss. Tissue Eng Part A 23:556–571. https://doi.org/10.1089/ten.tea.2016.0458CrossRef

18.

Apel PJ, Garrett JP, Sierpinski P, Ma J, Atala A, Smith TL et al (2008) Peripheral nerve regeneration using a keratin-based scaffold: long-term functional and histological outcomes in a mouse model. J Hand Surg 33:1541–1547. https://doi.org/10.1016/j.jhsa.2008.05.034CrossRef

19.

Pace LA, Plate JF, Mannava S, Barnwell JC, Koman LA, Li Z et al (2013) A human hair keratin hydrogel scaffold enhances median nerve regeneration in nonhuman primates: an electrophysiological and histological study. Tissue Eng Part A. https://doi.org/10.1089/ten.tea.2013.0084CrossRef

20.

Hill PS, Apel PJ, Barnwell J, Smith T, Koman LA, Atala A et al (2011) Repair of peripheral nerve defects in rabbits using keratin hydrogel scaffolds. Tissue Eng Part A 17:1499–1505. https://doi.org/10.1089/ten.tea.2010.0184CrossRef

21.

Sadeghi S, Nourmohammadi J, Ghaee A, Soleimani N (2020) Carboxymethyl cellulose-human hair keratin hydrogel with controlled clindamycin release as antibacterial wound dressing. Int J Biol Macromol 147:1239–1247. https://doi.org/10.1016/j.ijbiomac.2019.09.251CrossRef

22.

Li W, Gao F, Kan J, Deng J, Wang B, Hao S et al (2019) Synthesis and fabrication of a keratin-conjugated insulin hydrogel for the enhancement of wound healing. Colloids Surf B Biointerfaces 175:436–444. https://doi.org/10.1016/j.colsurfb.2018.12.020CrossRef

23.

Xu S, Sang L, Zhang Y, Wang X, Li X (2013) Biological evaluation of human hair keratin scaffolds for skin wound repair and regeneration. Mater Sci Eng C 33:648–655. https://doi.org/10.1016/j.msec.2012.10.011CrossRef

24.

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 42:541–547. https://doi.org/10.1016/j.burns.2015.10.024CrossRef

25.

Li Q, Zhu L, Liu R, Huang D, Jin X, Che N et al (2012) Biological stimuli responsive drug carriers based on keratin for triggerable drug delivery. J Mater Chem 22:19964. https://doi.org/10.1039/c2jm34136kCrossRef

26.

Xu H, Yang Y (2014) Controlled de-cross-linking and disentanglement of feather keratin for fiber preparation via a novel process. ACS Sustain Chem Amp Eng 2:1404–1410. https://doi.org/10.1021/sc400461dCrossRef

27.

de Souza FD, Benvenuti J, Meyer M, Wulf H, Klüver E, Gutterres M (2020) Extraction of keratin from unhairing of bovine hide. Chem Eng Commun 209:1–9. https://doi.org/10.1080/00986445.2020.1842740CrossRef

28.

Food and Agriculture Organization of the United Nations (FAO) (2020) World Food and Agriculture—Statistical Yearbook 2020. https://www.fao.org/documents/card/en/c/cb1329en/. Accessed Jan 2021

29.

Mokrejš P, Huťťa M, Pavlačková J, Egner P (2017) Preparation of keratin hydrolysate from chicken feathers and its application in cosmetics. J Vis Exp 129:56254. https://doi.org/10.3791/56254CrossRef

30.

Petek B, Marinšek Logar R (2021) Management of waste sheep wool as valuable organic substrate in European Union countries. J Mater Cycles Waste Manag 23:44–54. https://doi.org/10.1007/s10163-020-01121-3CrossRef

31.

Wang D, Yang XH, Tang RC, Yao F (2018) Extraction of keratin from rabbit hair by a deep eutectic solvent and its characterization. Polymers 10:993–993. https://doi.org/10.3390/polym10090993CrossRef

32.

Thankaswamy SR, Sundaramoorthy S, Palanivel S, Ramudu KN (2018) Improved microbial degradation of animal hair waste from leather industry using Brevibacterium luteolum (MTCC 5982). J Clean Prod 189:701–708. https://doi.org/10.1016/j.jclepro.2018.04.095CrossRef

33.

Gupta A (2014) Human hair “waste” and its utilization: gaps and possibilities. J Waste Manag 2014:1–17. https://doi.org/10.1155/2014/498018CrossRef

34.

Reddy CC, Khilji IA, Gupta A, Bhuyar P, Mahmood S, Al-Japairai KA et al (2021) Valorization of keratin waste biomass and its potential applications. J Water Process Eng 40:101707. https://doi.org/10.1016/j.jwpe.2020.101707CrossRef

35.

Nakamura A, Arimoto M, Takeuchi K, Fujii T (2002) A rapid extraction procedure of human hair proteins and identification of phosphorylated species. Biol Pharm Bull 25:569–572. https://doi.org/10.1248/bpb.25.569CrossRef

36.

Agarwal V, Panicker AG, Indrakumar S, Chatterjee K (2019) Comparative study of keratin extraction from human hair. Int J Biol Macromol 133:382–390. https://doi.org/10.1016/j.ijbiomac.2019.04.098CrossRef

37.

Jin X, Wang Y, Yuan J, Shen J (2016) Extraction, characterization, and NO release potential of keratin from human hair. Mater Lett 175:188–190. https://doi.org/10.1016/j.matlet.2016.04.036CrossRef

38.

Zhang L, Zhu P, Ying Sui S, Hong Dong C, Tao XuJ (2015) Study on the extraction and properties of human hair proteins. Integr Ferroelectr 160:169–174. https://doi.org/10.1080/10584587.2015.1033370CrossRef

39.

Shin S, Lee A, Lee S, Lee K, Kwon J, Yoon MY et al (2010) Microwave-assisted extraction of human hair proteins. Anal Biochem 407:281–283. https://doi.org/10.1016/j.ab.2010.08.021CrossRef

40.

Wong SY, Lee CC, Ashrafzadeh A, Junit SM, Abrahim N, Hashim OH (2016) A high-yield two-hour protocol for extraction of human hair shaft proteins. PLoS ONE 11:e0164993–e0164993. https://doi.org/10.1371/journal.pone.0164993CrossRef

41.

Fujii T, Takayama S, Ito Y (2013) A novel purification procedure for keratin-associated proteins and keratin from human hair. J Biol Macromol 13:92–106. https://doi.org/10.14533/jbm.13.92CrossRef

42.

Lee YJ, Rice RH, Lee YM (2006) Proteome analysis of human hair shaft: from protein identification to posttranslational modification. Mol Amp Cell Proteom 5:789–800. https://doi.org/10.1074/mcp.M500278-MCP200CrossRef

43.

Carracedo A, Concheiro L, Requena I (1985) The isoelectric focusing of keratins in hair followed by silver staining. Forensic Sci Int 29:83–89. https://doi.org/10.1016/0379-0738(85)90033-7CrossRef

44.

Gillespie JM, Marshall RC (1977) Proteins of the hard keratins of echidna, hedgehog, rabbit, ox and man. Aust J Biol Sci 30:401–410. https://doi.org/10.1071/BI9770401CrossRef

45.

Marshall RC, Gillespie JM (1977) The keratin proteins of wool, horn and hoof from sheep. Aust J Biol Sci 30:389–400. https://doi.org/10.1071/BI9770389CrossRef

46.

Cassoni AC, Freixo R, Pintado AI, Amorim M, Pereira CD, Madureira AR et al (2018) Novel eco-friendly method to extract keratin from hair. ACS Sustain Chem Amp Eng 6:12268–12274. https://doi.org/10.1021/acssuschemeng.8b02680CrossRef

47.

Tasaki K (2020) A novel thermal hydrolysis process for extraction of keratin from hog hair for commercial applications. Waste Manag 104:33–41. https://doi.org/10.1016/j.wasman.2019.12.042CrossRef

48.

Li QF, He Y, Wang RM (2019) A facile extraction of keratin from pig hair and its properties. Biologia (Bratisl) 74:563–571. https://doi.org/10.2478/s11756-019-00210-CrossRef

49.

Gillespie JM, Frenkel MJ (1974) The diversity of keratins. Comp Biochem Physiol Part B Comp Biochem 47:339–346. https://doi.org/10.1016/0305-0491(74)90063-7CrossRef

50.

Gillespie JM (1972) Proteins rich in glycine and tyrosine from keratins. Comp Biochem Physiol Part B Comp Biochem 41:723–734. https://doi.org/10.1016/0305-0491(72)90085-5CrossRef

51.

Idris A, Vijayaraghavan R, Rana UA, Patti AF, Macfarlane DR (2014) Dissolution and regeneration of wool keratin in ionic liquids. Green Chem 16:2857–2864. https://doi.org/10.1039/C4GC00213JCrossRef

52.

Shavandi A, Bekhit AE, Carne A, Bekhit A (2017) Evaluation of keratin extraction from wool by chemical methods for bio-polymer application. J Bioact Compat Polym 32:163–177. https://doi.org/10.1177/0883911516662069CrossRef

53.

Ozaki Y, Takagi Y, Mori H, Hara M (2014) Porous hydrogel of wool keratin prepared by a novel method: an extraction with guanidine/2-mercaptoethanol solution followed by a dialysis. Mater Sci Eng C 42:146–154. https://doi.org/10.1016/j.msec.2014.05.018CrossRef

54.

Eslahi N, Dadashian F, Nejad NH (2013) An investigation on keratin extraction from wool and feather waste by enzymatic hydrolysis. Prep Biochem Biotechnol 43:624–648. https://doi.org/10.1080/10826068.2013.763826CrossRef

55.

Aluigi A, Tonetti C, Rombaldoni F, Puglia D, Fortunati E, Armentano I et al (2014) Keratins extracted from Merino wool and Brown Alpaca fibres as potential fillers for PLLA-based biocomposites. J Mater Sci 49:6257–6269. https://doi.org/10.1007/s10853-014-8350-9CrossRef

56.

Shavandi A, Carne A, Bekhit AA, Bekhit AE (2017) An improved method for solubilisation of wool keratin using peracetic acid. J Environ Chem Eng 5:1977–1984. https://doi.org/10.1016/j.jece.2017.03.043CrossRef

57.

Plowman JE, Clerens S, Lee E, Harland DP, Dyer JM, Deb-Choudhury S (2014) Ionic liquid-assisted extraction of wool keratin proteins as an aid to MS identification. Anal Methods 6:7305–7311. https://doi.org/10.1039/C4AY01251HCrossRef

58.

Rajabinejad H, Zoccola M, Patrucco A, Montarsolo A, Rovero G, Tonin C (2018) Physicochemical properties of keratin extracted from wool by various methods. Text Res J 88:2415–2424. https://doi.org/10.1177/0040517517723028CrossRef

59.

Su C, Gong JS, Qin J, He JM, Zhou ZC, Jiang M et al (2020) Glutathione enables full utilization of wool wastes for keratin production and wastewater decolorization. J Clean Prod. https://doi.org/10.1016/j.jclepro.2020.122092CrossRef

60.

Ramya KR, Thangam R, Madhan B (2020) Comparative analysis of the chemical treatments used in keratin extraction from red sheep’s hair and the cell viability evaluations of this keratin for tissue engineering applications. Process Biochem 90:223–232. https://doi.org/10.1016/j.procbio.2019.11.015CrossRef

61.

Isarankura Na Ayutthaya S, Tanpichai S, Wootthikanokkhan J (2015) Keratin extracted from chicken feather waste: extraction, preparation, and structural characterization of the keratin and keratin/biopolymer films and electrospuns. J Polym Environ 23:506–516. https://doi.org/10.1007/s10924-015-0725-8CrossRef

62.

Gao P, Liu Z, Wu X, Cao Z, Zhuang Y, Sun W (2014) Biosorption of chromium (VI) ions by deposits produced from chicken feathers after soluble keratin extraction. Clean-Soil Air Water 42:1558–1566. https://doi.org/10.1002/clen.201300669CrossRef

63.

Pourjavaheri F, Pour SO, Jones OA, Smooker PM, Brkljača R, Sherkat F et al (2019) Extraction of keratin from waste chicken feathers using sodium sulfide and l-cysteine. Process Biochem 82:205–214. https://doi.org/10.1016/j.procbio.2019.04.010CrossRef

64.

Kamarudin NB, Sharma S, Gupta A, Kee CG, Chik SM, Gupta R (2017) Statistical investigation of extraction parameters of keratin from chicken feather using design-expert. Biotech 7:127–127. https://doi.org/10.1007/s13205-017-0767-9CrossRef

65.

Paz-García EJ, Paredes-Carrera SP, Flores-Valle SO, Rodríguez-Clavel IS, Sánchez-Ochoa JC, Pérez-Gutiérrez RM (2019) Effect of microwave or ultrasound irradiation in the extraction from feather keratin. J Chem 16:5525. https://doi.org/10.3390/app9245525CrossRef

66.

Khumalo M, Sithole B, Tesfaye T (2020) Valorisation of waste chicken feathers: optimisation of keratin extraction from waste chicken feathers by sodium bisulphite, sodium dodecyl sulphate and urea. J Environ Manage 262:110329–110329. https://doi.org/10.1016/j.jenvman.2020.110329CrossRef

67.

Alahyaribeik S, Ullah A (2020) Methods of keratin extraction from poultry feathers and their effects on antioxidant activity of extracted keratin. Int J Biol Macromol 148:449–456. https://doi.org/10.1016/j.ijbiomac.2020.01.144CrossRef

68.

Sinkiewicz I, Śliwińska A, Staroszczyk H, Kołodziejska I (2017) Alternative methods of preparation of soluble keratin from chicken feathers. Waste Biomass Valoriz 8:1043–1048. https://doi.org/10.1007/s12649-016-9678-yCrossRef

69.

Ma B, Qiao X, Hou X, Yang Y (2016) Pure keratin membrane and fibers from chicken feather. Int J Biol Macromol 89:614–621. https://doi.org/10.1016/j.ijbiomac.2016.04.039CrossRef

70.

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 132:577–583. https://doi.org/10.1016/j.seppur.2014.05.049CrossRef

71.

Zhang Y, Zhao W, Yang R (2015) Steam flash explosion assisted dissolution of keratin from feathers. ACS Sustain Chem Amp Eng 3:2036–2042. https://doi.org/10.1021/acssuschemeng.5b00310CrossRef

72.

O’donnell IJ (1973) A search for a simple keratin-fractionation and peptide mapping of proteins from feather keratins. Aust J Biol Sci 26:401–414. https://doi.org/10.1071/BI9730401CrossRef

73.

Harrap BS, Woods EF (1967) Species differences in the proteins of feathers. Comp Biochem Physiol 20:449–460. https://doi.org/10.1016/0010-406X(67)90260-5CrossRef

74.

Akahane K, Murozono S, Murayama K (1977) Soluble proteins from fowl feather keratin: I. Fractionation Prop J Biochem (Tokyo) 81:11–18. https://doi.org/10.1093/oxfordjournals.jbchem.a131425CrossRef

75.

Fuchs E, Hanukoglu I (1986) Epidermal α-keratins: structural diversity and changes during tissue differentiation. In: Bereiter-Hahn J, Matoltsy AG, Richards KS (eds) Biology of the integument. Springer, Heidelberg, pp 644–665CrossRef

76.

Matoltsy AG, Balsamo CA (1955) A study of the components of the cornified epithelium of human skin. J Cell Biol 1:339–360. https://doi.org/10.1083/jcb.1.4.339CrossRef

77.

Eichner R, Kahn M (1990) Differential extraction of keratin subunits and filaments from normal human epidermis. J Cell Biol 110:1149–1168. https://doi.org/10.1083/jcb.110.4.1149CrossRef

78.

Sun TT, Green H (1978) Keratin filaments of cultured human epidermal cells. Formation of intermolecular disulfide bonds during terminal differentiation. J Biol Chem 253:2053–2060. https://doi.org/10.1016/S0021-9258(19)62353-7CrossRef

79.

Steinert PM (1975) The extraction and characterization of bovine epidermal α-keratin. Biochem J 149:39–48. https://doi.org/10.1042/bj1490039CrossRef

80.

Skerrow D (1986) Epidermal α-keratin: structure and chemical composition. In: Bereiter-Hahn J, Matoltsy AG, Richards KS (eds) Biology of the integument. Springer, Heidelberg, pp 621–643CrossRef

81.

Zhang QB, Li C, Pan YT, Shan GH, Cao P, He J (2013) Microstructure and mechanical properties of horns derived from three domestic bovines. Mater Sci Eng C 33:5036–5043. https://doi.org/10.1016/j.msec.2013.08.034CrossRef

82.

Srinivasan B, Kumar R, Shanmugam K, Sivagnam UT, Reddy NP, Sehgal PK (2010) Porous keratin scaffold-promising biomaterial for tissue engineering and drug delivery. J Biomed Mater Res Part B Appl Biomater 92:5–12. https://doi.org/10.1002/jbm.b.31483CrossRef

83.

Fraser RDB, Parry DAD (2017) Filamentous structure of hard β-keratins in the epidermal appendages of birds and reptiles. In: Parry D, Squire J (eds) Fibrous proteins: structures and mechanisms subcellular biochemistry. Springer, Cham, pp 231–252CrossRef

84.

Gillespie JM, Marshall RC, Woods EF (1982) A comparison of lizard claw keratin proteins with those of avian beak and claw. J Mol Evol 18:121–129. https://doi.org/10.1007/BF01810831CrossRef

85.

Kakkar P, Madhan B, Shanmugam G (2014) Extraction and characterization of keratin from bovine hoof: a potential material for biomedical applications. Springerplus 3:596–596. https://doi.org/10.1186/2193-1801-3-596CrossRef

86.

Grosenbaugh DA, Hood DM (1992) Keratin and associated proteins of the equine hoof wall. Am J Vet Res 53:1859–1863

87.

Seki Y, Kad B, Benson D, Meyers MA (2006) The toucan beak: structure and mechanical response. Mater Sci Eng C 26:1412–1420. https://doi.org/10.1016/j.msec.2005.08.025CrossRef

88.

Frenkel MJ, Gillespie JM (1976) The proteins of the keratin component of bird? s beaks. Aust J Biol Sci 29:467–480. https://doi.org/10.1071/BI9760467CrossRef

89.

Spitzer RH, Downing SW, Koch EA, Salo WL, Saidel LJ (1984) Hagfish slime gland thread cells. II. Isolation and characterization of intermediate filament components associated with the thread. J Cell Biol 98:670–677. https://doi.org/10.1083/jcb.98.2.670CrossRef

90.

Bal Altuntaş D, Nevruzoğlu V, Dokumacı M, Cam Ş (2020) Synthesis and characterization of activated carbon produced from waste human hair mass using chemical activation. Carbon Lett 30:307–313. https://doi.org/10.1007/s42823-019-00099-9CrossRef

91.

Marshall RC, Gillespie JM (1982) Comparison of samples of human hair by two-dimensional electrophoresis. J Forensic Sci Soc 22:377–385. https://doi.org/10.1016/S0015-7368(82)71515-4CrossRef

92.

He J, Xu D, Li J, Li L, Li W, Cui W et al (2020) Highly efficient extraction of large molecular-weight keratin from wool in a water/ethanol co-solvent. Text Res J 90:1084–1093. https://doi.org/10.1177/0040517519885022CrossRef

93.

Allafi F, Hossain MS, Lalung J, Shaah M, Salehabadi A, Ahmad MI et al (2022) Advancements in applications of natural wool fiber: review. J Nat Fibers 19:497–512. https://doi.org/10.1080/15440478.2020.1745128CrossRef

94.

Kumar SL, Anandhavelu S, Sivaraman J, Swathy M (2017) Modified extraction and characterization of keratin from Indian goat hoof: a biocompatible biomaterial for tissue regenerative applications. Integr Ferroelectr 184:41–49. https://doi.org/10.1080/10584587.2017.1368642CrossRef

95.

Reichl S (2009) Films based on human hair keratin as substrates for cell culture and tissue engineering. Biomaterials 30:6854–6866. https://doi.org/10.1016/j.biomaterials.2009.08.051CrossRef

96.

Wang Y, Misto M, Yang J, Gehring N, Yu X, Moussian B (2021) Toxicity of dithiothreitol (DTT) to drosophila melanogaster. Toxicol Rep 8:124–130. https://doi.org/10.1016/j.toxrep.2020.12.014CrossRef

97.

Lee H, Noh K, Lee SC, Kwon IK, Han DW, Lee IS et al (2014) Human hair keratin and its-based biomaterials for biomedical applications. Tissue Eng Regen Med 11:255–265. https://doi.org/10.1007/s13770-014-0029-4CrossRef

98.

Lee H, Hwang YS, Lee HS, Choi S, Kim SY, Moon JH (2015) Human hair keratin-based biofilm for potent application to periodontal tissue regeneration. Macromol Res 23:300–308. https://doi.org/10.1007/s13233-015-3036-yCrossRef

99.

Hill P, Brantley H, Van Dyke M (2010) Some properties of keratin biomaterials: kerateines. Biomaterials 31:585–593. https://doi.org/10.1016/j.biomaterials.2009.09.076CrossRef

100.

Yamauchi K, Maniwa M, Mori T (1998) Cultivation of fibroblast cells on keratin-coated substrata. J Biomater Sci Polym Ed 9:259–270. https://doi.org/10.1163/156856298X00640CrossRef

101.

Fraser RB, Parry DA (2008) Molecular packing in the feather keratin filament. J Struct Biol 162:1–13. https://doi.org/10.1016/j.jsb.2008.01.011CrossRef

102.

Fudge DS, Winegard T, Ewoldt RH, Beriault D, Szewciw L, Douglas MGH, Fudge S, Winegard GMT, Ewoldt RH, Beriault D, Szewciw L (2009) From ultra-soft slime to hard α-keratins: the many lives of intermediate filaments. Integr Comp Biol 49:32–39. https://doi.org/10.1093/icb/icp007CrossRef

103.

Kitahara T, Ogawa H (1991) The extraction and characterization of human nail keratin. J Dermatol Sci 2:402–406. https://doi.org/10.1016/0923-1811(91)90003-GCrossRef

Title: Extraction of keratin from keratinous wastes: current status and future directions
Authors: Neeharika Senthilkumar
Snehaunshu Chowdhury
Pallab Sanpui
Publication date: 06-10-2022
Publisher: Springer Japan
Published in: Journal of Material Cycles and Waste Management / Issue 1/2023
Print ISSN: 1438-4957
Electronic ISSN: 1611-8227
DOI: https://doi.org/10.1007/s10163-022-01492-9

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